ID ANFD_AZOVI STANDARD; PRT; 517 AA. AC P16266; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 2. DT 07-FEB-2006, entry version 48. DE Nitrogenase iron-iron protein alpha chain (EC 1.18.6.1) (Nitrogenase DE component I) (Dinitrogenase 3 alpha subunit). GN Name=anfD; OS Azotobacter vinelandii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89123105; PubMed=2644222; RA Joerger R.D., Jacobson M.R., Premakumar R., Wolfinger E.D., RA Bishop P.E.; RT "Nucleotide sequence and mutational analysis of the structural genes RT (anfHDGK) for the second alternative nitrogenase from Azotobacter RT vinelandii."; RL J. Bacteriol. 171:1075-1086(1989). RN [2] RP PROTEIN SEQUENCE OF 1-6. RC STRAIN=RP306; RX MEDLINE=93319493; PubMed=8392330; RA Pau R.N., Eldridge M.E., Lowe D.J., Mitchenall L.A., Eady R.R.; RT "Molybdenum-independent nitrogenases of Azotobacter vinelandii: a RT functional species of alternative nitrogenase-3 isolated from a RT molybdenum-tolerant strain contains an iron-molybdenum cofactor."; RL Biochem. J. 293:101-107(1993). CC -!- FUNCTION: This iron-iron protein is part of the nitrogenase CC complex that catalyzes the key enzymatic reactions in nitrogen CC fixation. Other nitrogenase complexes utilize a molybdenum-iron CC protein or a vanadium-iron protein. CC -!- CATALYTIC ACTIVITY: 8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP CC + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16 CC phosphate. CC -!- COFACTOR: Binds 1 8Fe-7S cluster per heterodimer (By similarity). CC -!- COFACTOR: Binds 1 8Fe-9S-X-homocitryl cluster per subunit (By CC similarity). CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains. CC -!- SIMILARITY: Belongs to the nifD/nifK/nifE/nifN family. CC -!- CAUTION: The structure of the 8Fe-9S-X-homocitryl cluster is CC assumed to be analogous to the 7Fe-Mo-9S-X-homocitryl cluster. The CC identity of the X atom is not known, possibly carbon or oxygen. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M23528; AAA82509.1; -; Genomic_DNA. DR PIR; B32057; B32057. DR HSSP; P00467; 1MIO. DR InterPro; IPR011290; ANFD. DR InterPro; IPR010143; N2-ase-Ialpha. DR InterPro; IPR005974; Nitrog_alpha. DR InterPro; IPR000318; Nitrognse_comp1. DR InterPro; IPR000510; Oxred_nitrognse1. DR Pfam; PF00148; Oxidored_nitro; 1. DR TIGRFAMs; TIGR01284; alt_nitrog_alph; 1. DR TIGRFAMs; TIGR01861; ANFD; 1. DR TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1. DR PROSITE; PS00699; NITROGENASE_1_1; 1. DR PROSITE; PS00090; NITROGENASE_1_2; 1. KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; KW Nitrogen fixation; Oxidoreductase. FT INIT_MET 0 0 FT CHAIN 1 517 Nitrogenase iron-iron protein alpha FT chain. FT /FTId=PRO_0000153059. FT METAL 48 48 Iron-sulfur (8Fe-7S) (shared with beta FT chain) (By similarity). FT METAL 74 74 Iron-sulfur (8Fe-7S) (shared with beta FT chain) (By similarity). FT METAL 137 137 Iron-sulfur (8Fe-7S) (shared with beta FT chain) (By similarity). FT METAL 256 256 Iron-sulfur (8Fe-9S-X-homocitryl) (By FT similarity). FT METAL 422 422 Iron-sulfur (8Fe-9S-X-homocitryl) (via FT pros nitrogen) (By similarity). FT CONFLICT 3 3 H -> E (in Ref. 2). SQ SEQUENCE 517 AA; 58282 MW; D84B513BD2E66F8B CRC64; PHHEFECSKV IPERKKHAVI KGKGETLADA LPQGYLNTIP GSISERGCAY CGAKHVIGTP MKDVIHISHG PVGCTYDTWQ TKRYISDNDN FQLKYTYATD VKEKHIVFGA EKLLKQNIIE AFKAFPQIKR MTIYQTCATA LIGDDINAIA EEVMEEMPEV DIFVCNSPGF AGPSQSGGHH KINIAWINQK VGTVEPEITG DHVINYVGEY NIQGDQEVMV DYFKRMGIQV LSTFTGNGSY DGLRAMHRAH LNVLECARSA EYICNELRVR YGIPRLDIDG FGFKPLADSL RKIGMFFGIE DRAKAIIDEE VARWKPELDW YKERLMGKKV CLWPGGSKLW HWAHVIEEEM GLKVVSVYIK FGHQGDMEKG IARCGEGTLA IDDPNELEGL EALEMLKPDI ILTGKRPGEV AKKVRVPYLN AHAYHNGPYK GFEGWVRFAR DIYNAIYSPI HQLSGIDITK DNAPEWGNGF RTRQMLSDGN LSDAVRNSET LRQYTGGYDS VSKLREREYP AFERKVG //