ID Q1QW91_CHRSD Unreviewed; 953 AA.
AC Q1QW91;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:ABE59267.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:ABE59267.1};
GN OrderedLocusNames=Csal_1915 {ECO:0000313|EMBL:ABE59267.1};
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE59267.1, ECO:0000313|Proteomes:UP000000239};
RN [1] {ECO:0000313|EMBL:ABE59267.1, ECO:0000313|Proteomes:UP000000239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11
RC {ECO:0000313|Proteomes:UP000000239};
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE59267.1; -; Genomic_DNA.
DR RefSeq; WP_011507213.1; NC_007963.1.
DR AlphaFoldDB; Q1QW91; -.
DR STRING; 290398.Csal_1915; -.
DR KEGG; csa:Csal_1915; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_1_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000000239; 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: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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 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 PIRSF; PIRSF036643; FDH_alpha; 2.
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 ECO:0000313|EMBL:ABE59267.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000239};
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 953 AA; 106420 MW; C5E356C35450C96A CRC64;
MRLTRKSSQP AGQGGLGISR RQFLQRSGVA TGGLAAAGFM GHGMMQAASA KEKTAYSDAP
VETKRTICSH CSVGCGVYAE VQEGVWTKQE PAFDHPINRG AHCAKGASLR EHGHSTQRLK
YPMKLVDGKW QRLEWDQAIE EIGDKVLELR EQHGPDSVYW LGSAKFSNEQ AYLMRKLASL
WGTNNTDHQA RICHSTTVAG VANTWGYGAM TNSLNDMHFS KSILFIGSNP SEAHPVAMQH
ILHAKERNQA QIIVVDPRFT RTAAKANKYV RLRPGSDVAY IWGLLWHIFE NGWEDQQFID
QRVFGMDEVR REVAQFTPDV VERITGVSEA DMYDVAKRIS ENRPGCVVWC MGGTQHTTGN
NNTRAYCILE LALGNIGVSG GGANIFRGHD NVQGATDLGL GSDSLPGYYG LSEGAWQHWA
KVWNVDYEWI KNRYDQTEYN GALPMNSNGI TVSRWVDGVL EEDEHIAQRS SLKAMFYWGH
AVNSQTRGPE MKKAMSQLEL MVVVDPYPTV AAVMHDRTDG VYLLPAATQF ETTGSVTATN
RSLQWRDQVI EPMFDSKPDH EIMYLMAQKL GFGDEFTRNF AIEDGRPVIE DVLREINAGM
WTVGYTGQSP ERLKEHQKNW HTFNFDTLKA EGGPSDGDFY GLPWPCWGKP GMKHPGSPNL
YDISKSVAEG GMPFRARFGI EHEGQPLLAD GSYSKDSELN DGYPEFTSDM LKQLGWWDDL
TAEEKAAAEG KNWKTDLSGG IQRVAIAHGC APYGNAKARC RVWTFPDEVP KHREPLYTSR
RDLADEYPTW DDKASLFRLP TLYRSIQEKD FSKEFPIILT SGRLVEYEGG GEETRSMSWL
AELQQEMFVE INPAQANDLG IKNDDMVWVH GPEGGKVKVK AMVTPRVARD VAFMPFHFGG
VYQGESLADK YPEGARPYVL GEAANTATTY GYDPVTLMQE TKCTLCRIEK ASA
//
