ID A0A090ALQ2_9GAMM Unreviewed; 897 AA.
AC A0A090ALQ2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Anaerobic dehydrogenase {ECO:0000313|EMBL:BAP56075.1};
GN ORFNames=THII_1778 {ECO:0000313|EMBL:BAP56075.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP56075.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP56075.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
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 -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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DR EMBL; AP014633; BAP56075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090ALQ2; -.
DR STRING; 40754.THII_1778; -.
DR KEGG; tig:THII_1778; -.
DR HOGENOM; CLU_000422_13_4_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000031623; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR CDD; cd02754; MopB_Nitrate-R-NapA-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; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
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 PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04324; Fer2_BFD; 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.
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 Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031623}.
FT DOMAIN 1..54
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 897 AA; 99024 MW; 53A5407291E461E2 CRC64;
MVQTTCPYCG VGCGITAEVN QHTVTIKGDK THPANFGRLC SKGAALADTL DLNDRLLYPE
LHHQRVSWET ALTKVANEFK RIIREHGANA IAFYVSGQLL TEDYYVANKL MKGFLGTANI
DTNSRLCMAS SVAGHKRAFG SDTVSGCYED LELADLVVLV GSNLAWCHPV LYQRLAAAKE
QRPRLKIVVI DPRYTATSDI ADLHLPIRSG TDVWLFNGLL NFLRTHDHLD YEFLEAHTHG
AGAALKSARE SAATIPQIAQ LCGLTEMDVA EFYRLFAKTD KTVTVYSQGV NQSSAGTDKV
NSIINCHLAT GRIGKPGATP FSVTGQPNAM GGREVGALAN QLVAHLDFKP EHLALVQQFW
QSPVIAQQPG LKAVELYDAI VAGQIKAIWI MATNPVVSLP HADKVKQALG MCELVVVSDC
VRYTDTTEFA HVLLPALAWG EKEGTVTNSE RRISRQRAFL PVPGDAKPDW WIITEVARRL
GFAETAFAYQ SSADIFREYA ALSGEQNKGT RDFDISGLAN LSDADYQRLS PVQWPLKSPT
EVGTTRLFSD YQFFTADNKA HLIAIMPRAP VHLPNRDYPF ILNTGRTRDQ WHTMTRTGKS
ARLLSHTSES YVEIHPQDAG LLRIQVGDLV TVSSELGQVV VRVKISDHQQ PGNVFIPMHW
NGQNSSQARV GALIPPVTDP ISGQPEFKHT PVKVERYQPA WYGFLLSSTE LDAPSNQETS
AQPFSKITLH EVADYWVKVR EVAGWRYELA GQRRIDWSLW VRQQLGTEDW LEFQDRAQGR
YRCANIVNEQ LNICLFIGAE ARLTSRKPLM SLFGKTLDPV ERLRLLTGEP NSAPAASGEV
ICACHAVGRE TILAAIRQHG LVNYQQIGET LKAGTGCGSC IPELKALLIE AKGREVA
//