ID B8J7N7_ANAD2 Unreviewed; 1028 AA.
AC B8J7N7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:ACL67217.1};
DE Flags: Precursor;
GN OrderedLocusNames=A2cp1_3894 {ECO:0000313|EMBL:ACL67217.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL67217.1, ECO:0000313|Proteomes:UP000007089};
RN [1] {ECO:0000313|Proteomes:UP000007089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP001359; ACL67217.1; -; Genomic_DNA.
DR KEGG; acp:A2cp1_3894; -.
DR HOGENOM; CLU_000422_1_0_7; -.
DR Proteomes; UP000007089; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR CDD; cd02752; MopB_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Selenium {ECO:0000313|EMBL:ACL67217.1};
KW Selenocysteine {ECO:0000313|EMBL:ACL67217.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 43..106
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 857..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 196
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ACL67217.1"
SQ SEQUENCE 1028 AA; 113053 MW; FCA3316B466D6375 CRC64;
MSVTRRQFLQ LTAAGVGSTG LVALGFSPDR VLADVRNFKL SRTAETRNTC PYCSVGCGVI
LYTLGDRSKN AHSAVMHVEG DPDHPVNRGT LCPKGASLLD FVQSPNRLRY PEYRAPGSDK
WERVTWDWAL DRIARLMKDD RDKNFVAKNA AGVTVNRWPT VGLLAASASS NETGYITHKV
WRALGGVAID NQARVUHGPT VAGLAPTFGR GAMTNSWVDI KNANLVLVMG GNPAEAHPCG
FKWVVEAKAH NKAQLIVVDP RFTRTAAVAD VFAQIRPGTD IAFLGGVIRH LLEKDAIQKQ
YVTAYTNASL IVKEGYGFQD GLFSGYDEAK HTYDKSTWSY ETGPDGFARS DPTLQDPRCV
YQLMKKHYAR YTPKMVADIT GVPEAAFTRI CDAIATTSAP DRTMTALYAL GWTQHSVGSQ
NIRCIAMIQL LLGNVGMAGG GVNALRGHSN IQGLTDLGLL SDLLPGYLTV PRDADTDVET
YLAKRTPKPL RPGQMNYWQN YPKFYASLMK AWYGKAATKE NGWAYDYLPK LDKVYDILAV
FDLMHQGKVN GYLCQGFNPL ASIPNKPKLL ESLSKLKFLV TIDPLVTETS NFWQNHGDLN
PVESAKIQTE VFRLPSSCFA EEDGSLVNSG RTLQWHWKAA EPPGEAKGDP EIVAALFTRI
RALYEKEGGA FADPIRDLTW DYKIPRAPSA EELAREFNGK ALADVKDPKA DPKDPKAPLL
AKEGEQLATF AHLQDDGSTA SGNWLYCGSF TQAGNQMARR DVSDPSGLGV TPSWGWSWPA
NRRVLYNRAS CDPSGKPWDK NRKLVWWNGA KWVGHDVPDF KIDSKPEEGM SPFIMNPEGM
GRLFALDKMA EGPFPEHYEP FESPAASNAM HPKVGPNPAA RIFPGDKAQL GLPGEFPYAA
TTYRVVEHFH FWTKHARIPS VLQPELFIEL DEVLAGKKGI RSGDAVAVRS KRGRIVGKAV
VTKRIKPLKI AGQEVHTVGI PIHWGFNGLT KPGYISNTLT PFVGDANTQT PEFKAFLVDV
EKAAAGQV
//
