ID A0A1U7XH90_NICSY Unreviewed; 1356 AA.
AC A0A1U7XH90;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Abscisic-aldehyde oxidase-like {ECO:0000313|RefSeq:XP_009786314.1};
GN Name=LOC104234447 {ECO:0000313|RefSeq:XP_009786314.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009786314.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009786314.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009786314.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000256|ARBA:ARBA00004913}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006849}.
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DR RefSeq; XP_009786314.1; XM_009788012.1.
DR STRING; 4096.A0A1U7XH90; -.
DR GeneID; 104234447; -.
DR KEGG; nsy:104234447; -.
DR eggNOG; KOG0430; Eukaryota.
DR OrthoDB; 761229at2759; -.
DR Proteomes; UP000189701; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProt.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006124; P:ferredoxin metabolic process; IEA:UniProt.
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; 3.90.1170.50; 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; 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 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:SF133; ABSCISIC-ALDEHYDE OXIDASE-LIKE; 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; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 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; 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; 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; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR000127-3};
KW Alkaloid metabolism {ECO:0000256|ARBA:ARBA00022589};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000127-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000127-
KW 3}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000189701}.
FT DOMAIN 6..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 229..417
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 1286
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-1"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 53
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 115
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 162
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 164
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-3"
FT BINDING 351..355
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 407
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 432
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000127-2"
FT BINDING 792
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 823
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 936
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 1110
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 1356 AA; 148053 MW; F101388954E0A6F8 CRC64;
MEQRKGNLVF AVNGERFELP NINPSTTLLH FLRSETCFKS PKLGCGEGGC GACVVLVSKY
DPKLKKVEDY SVSSCLTLVC SLNGCSITTS EGLGNTRDGF HSIHERFAGF HASQCGFCTP
GMCMSFFSAL INADKGNKAD PLPGFSKLTS SEAEKSIAGN LCRCTGYRPI ADACKSFAAD
IDIEDLGFNS FWKKGDSKEM KISKLPPYDP TKNFSTYPEF LKNECTTNLD STRYPWYSPT
SIEELQSLLN SSVAENGASF KLVVGNTGTG YYKETQRYDH YVDLRYIPEL SIIKRDQTGI
EVGATVTISK LISFLKEENK GNLGPYGKLV SEKLVNHMEK IASPFVRNSA SVGGNLVMAQ
KNGFPSDIAT LFLGVGATVS LMTGHALEKL TWEELLSRPQ IDSRTVLLSV WIPFKEESSL
KTFSKFLFET YRAAPRPHGN AIAYVNAAFG VDVSLCHNGI LINDIQLAFG AYGTKHSTRG
KKVEEYLTGK ILNAHILSEA LKLVKLAVVP EDGALHPEYR SSLAVSYVFQ FLYPLVDVHS
AIFNGINDIS LEEVSKSSND GGISQGRKQS LLSSAKQVVE SSSEHYPVGE PMKKVGASMQ
AAGEAVYVDD IPSPPNCLHG AFIYSTKPLA GVKGIQLEYN SLTDGFTDII TFKDIPSGGS
NVGSITMFGP EPLFADDLAR CAGERIAVAV ADTQRSADVA ATTALVEYDT VNVNSPILTV
EEAVEKSSFF QIPPFLYPKQ VGDFSKGMAE ADHKILSAEV RLGSEYYFYM ETQTALAIPD
EDNCMVVYTS SQCPEYAQNV IASCLGVPEH NIRVITRRVG GGFGGKAVRA MPVSTACALA
AYKLRRPVRI YVNRNSDMIM TGGRHPMKVT YSVGFKSSGK ITALHLDILI NAGISEDISP
LLPSNVIKAI KKYDWGALSF DVKVCKTNLT SKSAMRAPGE VQGSYIAEAI IEHVASLLSK
EVDSVRNKNV HTFESINLFY DNIVTEVGEY TLPGIMDKLA VSSSFFQRSK MVEQFNQKNT
WKKKGISRLP IIFEAMQRPT PGKVSILSDG SIVVEVGGIE IGQGLWTKVR QMTAYALGLI
ESSWSEELVE KVRVIQADSL SLVQGGCTAG STTSESSCEA VRRCCSVLVE RLTPLKKQLQ
EQNGSLDWPT LIRQAQMQAV NLSASSYYVP ESSSMSYLNF GAAVSEVEID ILTGETTILQ
SDIIYDCGQS LNPAVDMGQI EGAYVQGIGF FMHEEYLTNE DGLMVSNSTW TYKIPTIDTI
PRNFNVHLVN SGHHEKRVLS SKASGEPPLL LAASVHCATR AAVKAAREQL KLWGKLDESA
SEFYLDVPAI LPVVKTQCGL DYVEKYLQSL LTQKSN
//
