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Database: UniProt
Entry: A0A1T4UAP4_9GAMM
LinkDB: A0A1T4UAP4_9GAMM
Original site: A0A1T4UAP4_9GAMM 
ID   A0A1T4UAP4_9GAMM        Unreviewed;       951 AA.
AC   A0A1T4UAP4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SKA49822.1};
GN   ORFNames=SAMN02745132_01233 {ECO:0000313|EMBL:SKA49822.1};
OS   Enterovibrio nigricans DSM 22720.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Enterovibrio.
OX   NCBI_TaxID=1121868 {ECO:0000313|EMBL:SKA49822.1, ECO:0000313|Proteomes:UP000190162};
RN   [1] {ECO:0000313|Proteomes:UP000190162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22720 {ECO:0000313|Proteomes:UP000190162};
RA   Varghese N., Submissions S.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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; FUXU01000010; SKA49822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4UAP4; -.
DR   OrthoDB; 9810782at2; -.
DR   Proteomes; UP000190162; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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   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   PIRSF; PIRSF036643; FDH_alpha; 3.
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   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          61..117
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   951 AA;  106158 MW;  73B554FB721ED8E7 CRC64;
     MKLTKRSDSV SKDEKQLGVS RRAFMRNSTL AAAGGVAAAG MFAPGMMKKA SAKDVDSSKP
     KEMKRTICTH CSVGCGVYAG VQDGVWTDQE PAFDHPFNAG GHCAKGAALR EHGHGARRLK
     YPMKLVDGKW QKISWDQAIT EVGDKVLEIR EKLGPDSIYF LGSAKFNNEQ AYLFRKMASL
     WGTNNVDHQA RICHSTTVAG VANTWGYGAM TNSFNDMHNC KSVLFIGSNP AEAHPVAMQH
     ILIAKEKNDC KIVVADPRRS RTAAKADHHF YLRPGTDIAV VWGLLWHIFK NNWEDKEFIH
     QRVFGMDEIR EEVAKWPPEV VERVSGATPE QMETAAKMLA QNRPGCVVWC MGGTQHTTGN
     NNTRAYCILE LALGNLGRAG GGANIFRGHD NVQGATDLGV LSHTLPGYYG LSEGAWKHWS
     KVWEVDFDWV KGRYDPSEYE GTYPMHSAGI PVSRWIDGVL EDKDKIAQKN NISAMFYWGH
     AVNSQTRGQD MRKAMNELEM MVIVDPYPTV AAVMNQRKNG VYLLPATTQF ETFGSVTASN
     RSIQWRDKVI EPLFDSKPDH EIMYLLSKKL GFSDQLFKNI QINGTEPVIE DITREFNRGM
     WTIGMTGQSP ERLKLHQQNW HTFNFTSLEA EGGPLNGETY GLPWPCWGTP ELGHPGSHIL
     YDTSKEVARG GGNFRARFGV EYEGKNLLAV DSYSKGCELE DGYPEFTDKM LKQLGWWDDL
     TAEEKAAAEG KNWKTDLSGG IQRVAIKHGC MPYGNAKARA IVWTFPDRVP LHREPLFTPR
     RDLIAEYPTW DDKADIYRLP TLYKSIQDID VASEYPIILT SGRIVEYEGG GEETRSNPWL
     ATLQREMFVE INIVDANNIG IKDGQDVWVE GAEKGRVKVK AMITPRVKEG LAFMPFHFGG
     VFEGESLLSK YPEGSQPYVV GEAANTATTY GYDPVTVMQE TKVTLCKISA A
//
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