ID E4YPL8_OIKDI Unreviewed; 1830 AA.
AC E4YPL8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Sorbitol dehydrogenase {ECO:0000256|ARBA:ARBA00026132};
DE AltName: Full=Polyol dehydrogenase {ECO:0000256|ARBA:ARBA00032485};
GN ORFNames=GSOID_T00030522001 {ECO:0000313|EMBL:CBY37414.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY37414.1};
RN [1] {ECO:0000313|EMBL:CBY37414.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004318}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004318}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; FN654970; CBY37414.1; -; Genomic_DNA.
DR Proteomes; UP000011014; Unassembled WGS sequence.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05285; sorbitol_DH; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR045306; SDH-like.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 300..327
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 387..414
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 431..460
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1130..1158
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1171..1199
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 147..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 402..464
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 147..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1830 AA; 207476 MW; 1F9BCDC90411E720 CRC64;
MKSFGVSPCF PPEIYIRPKQ ENIDESQKEF DWVNDLFSNL AEGVKLAKKC PICELVPKSN
KKIEKKIKQH IISRHKIAIY PCKGEADCSY ESPWPAELAE HVEEVHQRQL TEAEEQGSPY
PISVRKQNIR KELEKFYTKK REPDHFLKKK KKVEKKKDEK DAVQNEPPKL TLINNLFEPE
NSAEIKKSSE KPKEPEKNQP KTSEKDQPST SADTTLVTAP QQADSDDMGL DQVIKLTPRE
NFRLTRERVK PQPTPNDKVN CPFCKLEMTR RGIVQHVSHS HADQAEKFRK DKAYKEILPF
KCDSCKLQFA GKESLRKHFN ARGNQKSTCQ KPEDDPETID PVKNIEYNCP DPKCNFFGKL
QIILNHLFRH PEMNVKFRTK KSALLPVKCH ACSFHFTQRS SLQKHIEKNR CERNQMAVQE
QESRKNKDAF HHCPFKCGRL YTSKEKLEEH IEKHHEKEKE VESRIVSQNG SLLKQLKRDS
QTNKIICPFP ECLAHVSVSY SIFQTHIRKM HSRDEYAFFR MIPTTDSPFV CQKCSWAFTN
GAIKNHFHQV AAVCTKNRRT RDEIARKGLH ETIKLIFAEP DPSPERTPEE RIEQIFQKKR
AQLNSISQPD SQEDEPETSP ELSSPQKINE NAAEVSKRIE EDQNDEQQDE NNQNKKVNQN
NQTTTSILKV KPEPPSLAEI PEKNIDPAHS LKTVEASSSE IDQQSNFKNN SLTKMVPLLE
AKEEPKSAQT SFNSSIAESK VAESQSEDEN EAREAASRQT TEDALEHLRN AHYEKVQEIL
KKRKEEEERK KRESNYKIST LTKMAPLFEE KEEPKSSQTS LNSSIVESKK TESQSGDKSD
EPEAASREKT VDDPDPLQPL RDAHCSNVNA ILKKREEQQN RNGLLKIPSE EHEENNSLKR
KRDNQEAAEA EIPVKESDAS RIESENESPR GLVDPIKISA TVKSEHSAKS LTIPLKAISF
NQLSESGEPA TKKARHEDKP EESSDDKNSE PDSSEENLKD ENADPDEIVK GSFSSCEKYK
FKCSVDNACD VKCETLPELS THVQIDHSTS DYIRFRATTR YFQFQCEECG YRSLSKEQHE
RHKAAGQVKN CRKFSAFRFN FGISMECDGI PIIALKLSEC SQSAEVEILE KCELCSEIFP
DMSNLFAHML SVHGIEEYYR MRSSCKARLE FKCENCSWFF PSEDSIKSHS QRICSAQKEI
TKRIDGEGHE CPFCKVTLNG QELIKHVDEE HQDFVIIFRL KESKLLKVKC TKCGFHFIST
HEREMHNREQ CCQNIKAKRD FFLALDGPNE APTTPEPPQP KKATPAPNSP KSLASNSKSP
HLIIPNLSAL SPNMSLPAMN SPNNLASISP TLSMPKKQVT NQYFPNQLQH HQSLANALFA
SFQQSQPSPQ SAPNPFQNLQ QNMNFVQSSN QQTSQINRQM LQLDQPNRYG NSVIGTCSYC
FVPMRTREEM ARHGANMQDC LIFAQTCKRA SRLPCPYCGV EITGDSKVLQ KSMTVRKNMS
SMISIFFKDE VLLEMGSVGI CGSDVHYWTH GRIGDFIVNE PMILGHEASG KVIKAGKNVK
NLAIGDRVSI EPGYNLEADD YAKNGRYNLS DVFFCATPPD DGCLMKYYKH KASWCYKIPE
NMSYEEAAFI EPLSVGIHAC RRANVTLGDT VLITGCGPIG LVSLLVARAM GASKVLLTDM
NGDRLKKALE CGASDTIQVT REQTPEQIAA LVEEKLGGKP NITVECTGAE SCIQTGIYAT
KSGGCLLLVG LGKEMANIPI VNAAVREVDI RGVFRYCNTW PIAINMISSG QINVKPLVTH
RFELKDSLKA FETTRRGEGV KVMIKCLPDI
//
