ID A0A2Y9ACC9_9RHOB Unreviewed; 913 AA.
AC A0A2Y9ACC9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=CO or xanthine dehydrogenase, Mo-binding subunit {ECO:0000313|EMBL:SSA41616.1};
DE SubName: Full=CO/xanthine dehydrogenase Mo-binding subunit {ECO:0000313|EMBL:PWJ21206.1};
GN ORFNames=BCF38_102456 {ECO:0000313|EMBL:PWJ21206.1},
GN SAMN05421539_102456 {ECO:0000313|EMBL:SSA41616.1};
OS Jannaschia seohaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=475081 {ECO:0000313|EMBL:SSA41616.1, ECO:0000313|Proteomes:UP000251571};
RN [1] {ECO:0000313|EMBL:SSA41616.1, ECO:0000313|Proteomes:UP000251571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25227 {ECO:0000313|EMBL:SSA41616.1,
RC ECO:0000313|Proteomes:UP000251571};
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWJ21206.1, ECO:0000313|Proteomes:UP000245839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25227 {ECO:0000313|EMBL:PWJ21206.1,
RC ECO:0000313|Proteomes:UP000245839};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR EMBL; QGDJ01000002; PWJ21206.1; -; Genomic_DNA.
DR EMBL; UETC01000002; SSA41616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9ACC9; -.
DR OrthoDB; 9763985at2; -.
DR Proteomes; UP000245839; Unassembled WGS sequence.
DR Proteomes; UP000251571; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
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; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000245839}.
FT DOMAIN 8..84
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 913 AA; 95413 MW; BE784F292E4259B7 CRC64;
MDKPLAIGAV AFDLNGMPVT ARPRLGERLS HTLRERLDAR DVKVGCDAGD CGACTVLVDG
APVCACLMPT HAAEGREVKT LRGLAVDPLH ARLAEAFEAH GAAQCGICTP GMMVSALALL
SETPAPSEPE VMDALGGVLC RCTGYRKIVA AVVATGAKTA ARADEPAGPG HVGTAMRRVD
GAGKTAGTER FGDDVAPPDA LVLRVLRSPH ARAAFAFGDL DAWTRSTPGI VCVLTAADIP
GENRFGVIPA FADQPVFAEG EARFRGEAVA CIVGEPEAVA ALDEATIPID WSPRPAAETP
DLARAPGAPQ LHADRADNLM CTGFVACGDA EAALARADAV VEGRFTTSFV EHAYIEPEAG
YAEMQGERIA VHACTQAPMM DREALAAILG RPETDIRIVP TGVGGGFGSK LDLSVQPYLA
LAALKTGRPV RLAYSRAESM QSTTKRHPAD MRVRIGATSD GRLLGMRFDG DFDTGAYASW
GPTVATRVPV HASGPYRIAD YRAEARGIHT HNPPAGAFRG FGVPQAAVAQ ESLFDMLADR
LGLDRLEFRI RNALTDGQPT VCGQIFAQGV GIRACLEALR PAWTEERARQ RPHGARLRGV
GVAAGWYGCG NTSLPNPSTF KAGLTPDGRI VLHQGAMDIG QGASTVMAQI FATALGVEVA
DVTLIGADTD LTPDGGKTSA SRQTFVSGNA ARLAGESLRA AILARANAGE GAVIRRDAGA
LAITDGARTH RLDLTAMPAD PEGYVLRAEE TYDPPTKPLD ANGQGAPYAQ FGYAAHLAVV
EIDAAMGTVH PLRFVAAHDV GRAVNPLLIE GQVEGGIAQG LGMALMEEYL PGRTENLHDY
LIPTIGDMPP VETIIVECTD AHGPYGAKGL GEHVLIPTAP ALLNAIADAT GARMTRLPVT
PARLRAALLE AKP
//
