ID Q1YLF3_AURMS Unreviewed; 996 AA.
AC Q1YLF3;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Putative formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:EAS51778.1};
GN ORFNames=SI859A1_02594 {ECO:0000313|EMBL:EAS51778.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS51778.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS51778.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS51778.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(2008).
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:EAS51778.1}.
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DR EMBL; AAPJ01000001; EAS51778.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1YLF3; -.
DR HOGENOM; CLU_000422_1_1_5; -.
DR OrthoDB; 9816402at2; -.
DR BioCyc; AURANTIMONAS:SI859A1_02594-MONOMER; -.
DR Proteomes; UP000000321; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000000321};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 68..124
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 750..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 110763 MW; 9F14C925D4B367E9 CRC64;
MLRKKANGAA RSNRMASALS ELGTAAVDRR TFLKRSGLTI GGAAAVATLS GGMVRRAEAA
GETATGEMEI RKSVCTHCSV GCTVLAEVSN GVWVGQEPGF DSPFNLGAHC AKGASVREHA
HGERRLKYPM KLVGGKWQRI SWDEAINEIG DKMLEVREAA GPDSVYWLGS AKHSNEQSYL
IRKFAAYWGT NNIDHQARIC HSTTVAGVAN TWGYGAMTNS YNDIHNSRAI FLIGGNPAEA
HPVSLLHLLK AKEENNAPLI VCDPRFTRTA AHADEYVRFR PGTDVALIWG VLYHIFENGW
EDKEFINSRV WGMDQIRTEV ARWTPEEVER VTGVPGSQLQ RVARTMAESR PATLIWCMGG
TQHTNGNNNT RAYCILQLAL GNMGKAGGGT NIFRGHDNVQ GATDLGVLAD TLPGYYGLTA
GSWAHWARVW EEELDWLKGR FAVMPGAGDE GKDRLMMNET GIPVSRWIDG VLEARENLEQ
PDNTKVMVFW GHAPNSQTRL PEMQKAMGML EMLVVIDPYP TMTAVLQDRT DGVYLLPAST
QFETSGSVTA SNRSLQWREK VVEPLFESLP DHTIMHKFAE KFGFADRMFR NIEVKDGEPV
VEDITREFNR GMWTIGYTGQ SPERMKSHMQ NQHTFDRTTL RGVGGAHDGE FYGMPWPCWG
TAEMKHSGSA NLYDTSIPVA QGGMGFRARF GVERDGDNLL AEGSWPVGSE IEDGYPEFTF
AMLKELGWDK DLTPYERRYI DYVAGFADQR PNQGDDVGEQ SQTGEIDSDY DEKVGGVNWK
TDLSGGIQRV AIAHGCAPYG NAKARAVVWT FPDPVPIHRE PLYTPRRDLV TDYPTYEDKT
FWRVPTAYAS IQKNDYSKDF PMIMTSGRLV EYEGGGDETR SNPWLAELQQ DMFVEINPSD
ANDLGLRDRD TVWLHSPEGG KIRIMAMVTE RVGRGVVFTP FHFGGYFQGN DLRGKYPDGA
DPYVLGEACN TAQTYGYDSV TQMQETKTTL CRIERA
//
