ID B8IKP1_METNO Unreviewed; 914 AA.
AC B8IKP1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Aldehyde oxidase and xanthine dehydrogenase molybdopterin binding {ECO:0000313|EMBL:ACL56248.1};
GN OrderedLocusNames=Mnod_1247 {ECO:0000313|EMBL:ACL56248.1};
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL56248.1, ECO:0000313|Proteomes:UP000008207};
RN [1] {ECO:0000313|EMBL:ACL56248.1, ECO:0000313|Proteomes:UP000008207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC {ECO:0000313|Proteomes:UP000008207};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) 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; CP001349; ACL56248.1; -; Genomic_DNA.
DR RefSeq; WP_015927944.1; NC_011894.1.
DR AlphaFoldDB; B8IKP1; -.
DR STRING; 460265.Mnod_1247; -.
DR KEGG; mno:Mnod_1247; -.
DR eggNOG; COG1529; Bacteria.
DR eggNOG; COG2080; Bacteria.
DR HOGENOM; CLU_001681_2_3_5; -.
DR OMA; THYYQTV; -.
DR OrthoDB; 9763985at2; -.
DR Proteomes; UP000008207; Chromosome.
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 CDD; cd00207; fer2; 1.
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.
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; XANTHINE DEHYDROGENASE; 1.
DR PANTHER; PTHR11908:SF157; XANTHINE DEHYDROGENASE SUBUNIT D-RELATED; 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:UP000008207}.
FT DOMAIN 3..79
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 914 AA; 95564 MW; AD54F21BE5099C11 CRC64;
MTRDVTLLVN GVAHRVEAPP FASLADTLRE RLHLTGTKVG CEAGDCGACT VLLDGEQVCA
CLVPTGQAEG RAVTTIEGAD PSGLIDRLRE AFLAHGAAQC GICTPAMILA AADGLRRNPQ
ADRRAVEDAV GGVLCRCTGY VKIVDAIMDV ARGADAVLPV PEPGAAVGTR MARIDGRAKV
EGRDRFGADH QPEDALWLRL VRSPHAAARF TIGDLGPVLA RHPGLTRILT ARDIPGANSF
GVFPHIKDQP VLADGLVRMR GDPVAALVGT RAAVEGFPDA DLPLIYEVLP ALSGLEAALA
PGAPPIHAGV PDNVLTRGRL TRGDVAAGHA AGAATASGAF ETAFVEHAYV EPEAGFARRV
GDRIEVTACT QAPVMDQEDV ARVLGLPLAA VRIVPTACGG GFGGKLDVSL QPILAVAAWL
TRRPVRMIFT RTESMAATTK RHPARIRARL SADGQGRFTA FELDGDFNTG AYASWGPTVA
NRVPVHAPGP YRVPHVRNRT RAVYTNDTPA GAFRGFGVPQ ATIAAETLID DLAGMLGIDR
WTIRRRNALE AGDTTASGQV LHASAGLPEC LDALRDDFFR MAAEAEAFNA GSPRIRRGVG
LACMWYGCGN TSMSNPSRMR IVLGPDGTLT FLNGAVDIGQ GSSTVLLQIA ADALGLGPDR
FRSVIGDTDL TCDAGKTSAS RQTFVSGNAA RLAGEDLRRR ILSLANAGPQ ARLTLEGARL
TIADGPASRT IDLSSLPPDE TGAVFSGEGW YDPPTTALDA DGQGIPYATY GFAAQVAAVE
VDTVLATVRV TRIVAAHDVG RAVNPTLVEG QIHGGIAQGL GLALMEEFIP GRTENLHDYL
IPTAGDVPEI DVRIIEDPDP EGPYGAKGVG EPALVATAPA ILSGIRHATG ARLTRVPVLP
HRLHAALHGT EAAE
//