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Database: UniProt
Entry: A0A090ALQ2_9GAMM
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Original site: A0A090ALQ2_9GAMM 
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
//
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