ID A0A067LEI8_JATCU Unreviewed; 1240 AA.
AC A0A067LEI8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=JCGZ_23867 {ECO:0000313|EMBL:KDP42925.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP42925.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP42925.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP42925.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000127-2};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000256|PIRSR:PIRSR000127-3};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR000127-3};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000256|PIRSR:PIRSR000127-3};
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DR EMBL; KK914286; KDP42925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067LEI8; -.
DR STRING; 180498.A0A067LEI8; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 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 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; IPR036884; 2Fe-2S-bd_dom_sf.
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; 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 PANTHER; PTHR11908:SF163; ALD_XAN_DH_C2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR PIRSF; PIRSF000127; Xanthine_DH; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3};
KW FAD {ECO:0000256|PIRSR:PIRSR000127-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000127-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000127-3};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000127-
KW 3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000127-3};
KW Molybdenum {ECO:0000256|PIRSR:PIRSR000127-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138}.
FT DOMAIN 106..296
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 1172
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT BINDING 39
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 41
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 230..234
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 246
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 678
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 709
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 822
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 996
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
SQ SEQUENCE 1240 AA; 136022 MW; 5424868232E86D97 CRC64;
MSLFGALVKA EKTDRPEPSP GFSKLTVNEA EKAIAGNLCR CTGYRPIADA CKSFAADVDM
EDLGLNSFWK KGEPQEVKIG RMPPYNQEIC TFPEFLKTEV KFPLLLDSKR CSWHQPCSFE
ELQSLLKTFG NGPEFQMKLV VGNTGTGYYK EVEHYDKYID LRYIPELSRI RRDGTGIEIG
AAVTIFKVIE ALRELNKSEC EFSSESKMVF NKIADHLEKV ANKFVRNTGS IGGNLVMAQR
KSFPSDIATI LLAAGSYVHV ISGTVHEKLT LEEFLERPPL DSKSILSTVK IPNFEVIKDK
SRERNCNLIF ETYRAAPRPL GSALAYLNAA FLAQVSSSKS SGGIVLNSCQ LAFGAFGTKH
AIRARKVEEF LTGKLLTIGV IYEAIKLVRA TVVPEHGTPN PEYRSSLAVS FLFDFLGPLR
NIGSKGLLNG HDDISMSEEI KLKENHDKLD HVKSPSLLLS SKQVIQLNKQ YDPVGKPIAK
TGAFLQASGE AVYVDDIPSP RNCLHGAFIY STKPFAKVKS IKFNSESLPD GVTAVISFKD
IPKGGQNIGS LFAFGPEPLF AEELTQYAGE PLAFVLADTQ RNADIASKLA VVDYDLENLQ
PPILTVEEAI ERSSIFEVPP IIYPKQIGDV SKGMAEADNK ILSAEIKLGS QYYFYMENQT
ALAVPDEDNC MVVYSSNQAP EYAHTVIAKC LGVPEHNVRV LTRRVGGGFG GKALKAMPVA
TACALAAHKL QRPVRVYLNR HTDMIMVGGR HPMKITYSVG FKSNGKITAL KLDILINAGI
SIDVSPVMPK AIVSALKKYD WGALSFDIKV CKTNVVSKSA MRAPGDVQGS YIAEAIIENV
AAFLFISSDS VRAINLHTYN TLKLYYDLSA GEPLEYTLTS IWNKLATSSS FEQRTELIKE
FNRSNVWKKR GISRIPVVYE VGTRPTAGKV SILNDGSIVV EVGGLEIGQG LWTKVKQMVA
FALSSIKCDG AGDLLDKVRV IQSDTLSLTQ GGMTAGSTTS ESSCEAVRLC CNVLVERLMA
VKERLLAQMD SIKWEKLISQ AYLEAVHLSA NSYFVPESAS MEYLNYGAAA SEVEVDLLTG
HTTILRSDIL YDCGQSLNPA VDLGQIEGAF VQGIGFFMLE EHTTNSDGLV DAKGTWTYKI
PTIDTIPKQF NVEIINSGHH QNRVLSSKAS GEPPLLLAAS VHCATRAAIS EARKQLDSWG
CQDSSRSIFQ VDVPATMPTV KELCGLDIVE RYLQWKMEGN
//
