ID A0A1Y6IUW0_9VIBR Unreviewed; 480 AA.
AC A0A1Y6IUW0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=4-hydroxybenzoyl-CoA reductase subunit gamma {ECO:0000313|EMBL:SMS00791.1};
DE EC=1.3.7.9 {ECO:0000313|EMBL:SMS00791.1};
GN Name=hcrC {ECO:0000313|EMBL:SMS00791.1};
GN ORFNames=VIM7927_02062 {ECO:0000313|EMBL:SMS00791.1};
OS Vibrio mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=474394 {ECO:0000313|EMBL:SMS00791.1, ECO:0000313|Proteomes:UP000196125};
RN [1] {ECO:0000313|EMBL:SMS00791.1, ECO:0000313|Proteomes:UP000196125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7927 {ECO:0000313|EMBL:SMS00791.1,
RC ECO:0000313|Proteomes:UP000196125};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FXXI01000003; SMS00791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6IUW0; -.
DR OrthoDB; 9775084at2; -.
DR Proteomes; UP000196125; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR InterPro; IPR012175; Xanth_DH_ssu_bac.
DR InterPro; IPR014307; Xanthine_DH_ssu.
DR NCBIfam; TIGR02963; xanthine_xdhA; 1.
DR PANTHER; PTHR45444:SF3; ALDEHYDE OXIDASE_XANTHINE DEHYDROGENASE, MOLYBDOPTERIN BINDING PROTEIN; 1.
DR PANTHER; PTHR45444; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR PIRSF; PIRSF036557; XdhA_RC; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Membrane {ECO:0000256|ARBA:ARBA00022692};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SMS00791.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT DOMAIN 1..86
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 179..352
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 480 AA; 54043 MW; 28BC361B2EAA18F8 CRC64;
MLEVMINNQV VSIPSVSADM MLLTYLREHR ELKGTKEGCA SGDCGACTVV IVDRDEQNEL
RYRQINACIT PLHALHGKQI ITVEYLKQRE QLHPVQQAIV DRHGSQCGFC TPGFVMSLYA
LSKQKHKPDN PADFLAGNLC RCTGYGPLIE AANEIAAAKT SDPLDEYQAE VQHWMNHVPP
LNSDHYFTPE NRQQLAELRR AYPSAQLIAG GTDLSLEVTQ RMAPLPLLID VSNVDDMLTV
TETDSGWRIG AAIPMYQVHR FMQQNFPSTD EIIERLGSIT IRHRATLGGS LGHASPIGDI
APLLISLKGQ IEIDNGSERK LYAPEDYITG YRQTRLQGNE WISAIHLPKM DRQQKHAIYK
VSKRYEDDIA TVVLAINLTF DEHAQISHCI VAAGGVAAKS VRLTTLETVF LGRPLTQSLI
REVQALVPQV IHPLSDIRGS AQYRIRLVQN LLQRYYLEYK QLEYKHPEHQ QIKTRLTYHA
//
