ID A0A4R6VB52_9PAST Unreviewed; 1017 AA.
AC A0A4R6VB52;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Formate dehydrogenase (Quinone-dependent) catalytic subunit {ECO:0000313|EMBL:TDQ57361.1};
GN ORFNames=EDC45_1415 {ECO:0000313|EMBL:TDQ57361.1};
OS Mesocricetibacter intestinalis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mesocricetibacter.
OX NCBI_TaxID=1521930 {ECO:0000313|EMBL:TDQ57361.1, ECO:0000313|Proteomes:UP000295657};
RN [1] {ECO:0000313|EMBL:TDQ57361.1, ECO:0000313|Proteomes:UP000295657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28403 {ECO:0000313|EMBL:TDQ57361.1,
RC ECO:0000313|Proteomes:UP000295657};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDQ57361.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SNYQ01000005; TDQ57361.1; -; Genomic_DNA.
DR Proteomes; UP000295657; 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: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; IPR006655; Mopterin_OxRdtase_prok_CS.
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; PS00932; MOLYBDOPTERIN_PROK_3; 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 Reference proteome {ECO:0000313|Proteomes:UP000295657};
KW Selenium {ECO:0000313|EMBL:TDQ57361.1};
KW Selenocysteine {ECO:0000256|ARBA:ARBA00022933,
KW ECO:0000313|EMBL:TDQ57361.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1017
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020720681"
FT DOMAIN 43..106
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 196
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:TDQ57361.1"
SQ SEQUENCE 1017 AA; 113385 MW; C210FF57F997136B CRC64;
MQVTRRKFFK ICAGGMAGTS AAVLGFAPVN ALAAPRAYKL LNTQEVRNTC TYCSVGCGML
LHSLGDTARN AKRKLFHIEG DPDHPVSRGA LCPKGAGALD YVNSPNRLRY PEYRAPGSDK
WVRLSWEEAY QRIAKLMKED RDANFQEKNA AGVTVNRWLT TGMLAASAAS NEAGLLTQKW
ARSLGMLALD NQARVUHGPT VASLAPTFGR GAMTNHWCDI KNADLVVVMG GNAAEAHPVG
FRWAMEAKIH NKAKILAVDP RFHRTASVAD FYAPIRSGSD ITFLSGVIKY LLDNDKIQHE
YVKHYTNATF LVDEGFAFNE GLFTGYDEAK RSYDKKTWNY QFDENGYAKR DMSMQHPRCV
INLLKQHVSR YTPEMVERIC GTSQKDFLYF CEEVAKTAVP DKTMTILYAL GWTQHSVGAQ
NIRTMSMIQL LLGNIGMAGG GVNALRGHSN IQGLTDLGLL SQMLPGYIRL PHEKETTYED
FINAVTPKST LPNQVNYWQN TPKFFVSMMK SFYGDKATRE NGWGFDFLPK WDAVYDVLRF
FSMMDEGKVN GYICQGFNPV ASFPDKNKVV RSLSKLKFLI VMDPLATETA TFWQNHGEMN
DVDSASIQTE VFRLPTTCFA EEDGSIANSG RWLQWHWKGA DQPGEALPDV DILAGIREAM
LELYHKEGGR GIKPFEAMSW NYKAPHTPTP AELAQENNGF ALADLVDEKG NVIVKKGELL
SSFAQLRDDG STASACWIYS GQWTPKGNQM ANRDNSDPSG LGNTLGWAFA WPLNRRIIYN
RASADINGQP WDKHRQLIKW NGKNWNYIDI ADYGTAAPGT DTMPFIMQPE GVGRLFALDK
MAEGPFPEHY EPFETPLGTN PLHPNVVSNP AARVFKDDLA QMGKAESFPY VGTTYRLTEH
FHFWTKHALL NVIAQPEQFV EIGESLAAEK GIKQGDYVKV SSSRGYIKAV AVVTKRLKAL
KADGKDIHHI GIPLHWGYEG VGKKGYIANT LTPFVGDANS QTPEFKSFLV NIERVEA
//
