HIS6A_ARATH
ID HIS6A_ARATH Reviewed; 417 AA.
AC B9DHD3; Q6S4C1; Q6S4D6; Q949X3; Q9LD56;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Histidinol-phosphate aminotransferase 1, chloroplastic;
DE EC=2.6.1.9;
DE AltName: Full=Gene duplicate 1-B protein;
DE AltName: Full=Imidazole acetol-phosphate transaminase;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2196;
DE AltName: Full=Protein HISTIDINE BIOSYNTHESIS 6A;
DE Flags: Precursor;
GN Name=HISN6A; Synonyms=EMB2196, GD1-B, HPA1; OrderedLocusNames=At5g10330;
GN ORFNames=F18D22.100;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-119 (ISOFORM 1), TISSUE SPECIFICITY,
RP AND DIFFERENTIAL EXPRESSION.
RC STRAIN=cv. Co-1, cv. Es-0, cv. Ita-0, cv. Kas-1, cv. Kon,
RC cv. Landsberg erecta, cv. Li-3, cv. Lu-1, cv. Mt-0, cv. PHW-1, cv. PHW-33,
RC cv. Pla-0, cv. Pog-0, cv. Tsu-1, and cv. Wassilewskija;
RX PubMed=14671323; DOI=10.1073/pnas.2535513100;
RA Moore R.C., Purugganan M.D.;
RT "The early stages of duplicate gene evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15682-15687(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547652; DOI=10.1007/s00726-005-0247-0;
RA Stepansky A., Leustek T.;
RT "Histidine biosynthesis in plants.";
RL Amino Acids 30:127-142(2006).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17434988; DOI=10.1104/pp.107.096511;
RA Muralla R., Sweeney C., Stepansky A., Leustek T., Meinke D.;
RT "Genetic dissection of histidine biosynthesis in Arabidopsis.";
RL Plant Physiol. 144:890-903(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-41, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER CYS-40, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC ChEBI:CHEBI:57980; EC=2.6.1.9;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B9DHD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DHD3-2; Sequence=VSP_036337;
CC -!- TISSUE SPECIFICITY: Expressed in both vegetative and reproductive
CC tissues. {ECO:0000269|PubMed:14671323}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB96689.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL360334; CAB96689.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91523.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91524.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69216.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69217.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69218.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69219.1; -; Genomic_DNA.
DR EMBL; AY050832; AAK92767.1; -; mRNA.
DR EMBL; AY117255; AAM51330.1; -; mRNA.
DR EMBL; BX831512; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK317485; BAH20150.1; -; mRNA.
DR EMBL; AY470015; AAR85399.1; -; Genomic_DNA.
DR EMBL; AY470016; AAR85400.1; -; Genomic_DNA.
DR EMBL; AY470017; AAR85401.1; -; Genomic_DNA.
DR EMBL; AY470018; AAR85402.1; -; Genomic_DNA.
DR EMBL; AY470019; AAR85403.1; -; Genomic_DNA.
DR EMBL; AY470020; AAR85404.1; -; Genomic_DNA.
DR EMBL; AY470021; AAR85405.1; -; Genomic_DNA.
DR EMBL; AY470022; AAR85406.1; -; Genomic_DNA.
DR EMBL; AY470023; AAR85407.1; -; Genomic_DNA.
DR EMBL; AY470024; AAR85408.1; -; Genomic_DNA.
DR EMBL; AY470025; AAR85409.1; -; Genomic_DNA.
DR EMBL; AY470026; AAR85410.1; -; Genomic_DNA.
DR EMBL; AY470027; AAR85411.1; -; Genomic_DNA.
DR EMBL; AY470028; AAR85412.1; -; Genomic_DNA.
DR EMBL; AY470029; AAR85413.1; -; Genomic_DNA.
DR PIR; T50821; T50821.
DR RefSeq; NP_001031867.1; NM_001036790.2. [B9DHD3-1]
DR RefSeq; NP_001117584.1; NM_001124112.2. [B9DHD3-1]
DR RefSeq; NP_001319364.1; NM_001334509.1. [B9DHD3-1]
DR RefSeq; NP_001321653.1; NM_001334511.1. [B9DHD3-2]
DR RefSeq; NP_001321654.1; NM_001334510.1. [B9DHD3-2]
DR RefSeq; NP_001330915.1; NM_001343108.1. [B9DHD3-2]
DR RefSeq; NP_001330916.1; NM_001343107.1. [B9DHD3-2]
DR RefSeq; NP_001330917.1; NM_001343106.1. [B9DHD3-2]
DR RefSeq; NP_001330918.1; NM_001343105.1. [B9DHD3-2]
DR RefSeq; NP_177337.1; NM_105850.3.
DR RefSeq; NP_568226.1; NM_121071.4. [B9DHD3-1]
DR AlphaFoldDB; B9DHD3; -.
DR SMR; B9DHD3; -.
DR BioGRID; 16175; 2.
DR BioGRID; 28743; 2.
DR STRING; 3702.AT1G71920.2; -.
DR iPTMnet; B9DHD3; -.
DR PaxDb; B9DHD3; -.
DR EnsemblPlants; AT1G71920.2; AT1G71920.2; AT1G71920.
DR EnsemblPlants; AT1G71920.4; AT1G71920.4; AT1G71920. [B9DHD3-2]
DR EnsemblPlants; AT1G71920.5; AT1G71920.5; AT1G71920. [B9DHD3-2]
DR EnsemblPlants; AT1G71920.6; AT1G71920.6; AT1G71920.
DR EnsemblPlants; AT5G10330.1; AT5G10330.1; AT5G10330.
DR EnsemblPlants; AT5G10330.2; AT5G10330.2; AT5G10330.
DR EnsemblPlants; AT5G10330.4; AT5G10330.4; AT5G10330. [B9DHD3-2]
DR EnsemblPlants; AT5G10330.5; AT5G10330.5; AT5G10330. [B9DHD3-2]
DR EnsemblPlants; AT5G10330.6; AT5G10330.6; AT5G10330. [B9DHD3-2]
DR EnsemblPlants; AT5G10330.7; AT5G10330.7; AT5G10330. [B9DHD3-2]
DR GeneID; 830897; -.
DR GeneID; 843523; -.
DR Gramene; AT1G71920.2; AT1G71920.2; AT1G71920.
DR Gramene; AT1G71920.4; AT1G71920.4; AT1G71920. [B9DHD3-2]
DR Gramene; AT1G71920.5; AT1G71920.5; AT1G71920. [B9DHD3-2]
DR Gramene; AT1G71920.6; AT1G71920.6; AT1G71920.
DR Gramene; AT5G10330.1; AT5G10330.1; AT5G10330.
DR Gramene; AT5G10330.2; AT5G10330.2; AT5G10330.
DR Gramene; AT5G10330.4; AT5G10330.4; AT5G10330. [B9DHD3-2]
DR Gramene; AT5G10330.5; AT5G10330.5; AT5G10330. [B9DHD3-2]
DR Gramene; AT5G10330.6; AT5G10330.6; AT5G10330. [B9DHD3-2]
DR Gramene; AT5G10330.7; AT5G10330.7; AT5G10330. [B9DHD3-2]
DR KEGG; ath:AT1G71920; -.
DR KEGG; ath:AT5G10330; -.
DR Araport; AT5G10330; -.
DR TAIR; locus:2145382; AT5G10330.
DR eggNOG; KOG0633; Eukaryota.
DR InParanoid; B9DHD3; -.
DR OMA; IWLNANE; -.
DR PhylomeDB; B9DHD3; -.
DR UniPathway; UPA00031; UER00012.
DR PRO; PR:B9DHD3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B9DHD3; baseline and differential.
DR Genevisible; B9DHD3; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; TAS:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005861; HisP_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Amino-acid biosynthesis;
KW Aminotransferase; Chloroplast; Histidine biosynthesis; Plastid;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 41..417
FT /note="Histidinol-phosphate aminotransferase 1,
FT chloroplastic"
FT /id="PRO_0000013447"
FT MOD_RES 41
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..113
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036337"
FT CONFLICT 115
FT /note="K -> R (in Ref. 3; BX831512)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="A -> E (in Ref. 3; BX831512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46635 MW; 49CF343430F62AA5 CRC64;
MGVINVQGSP SFSIHSSESN LRKSRALKKP FCSIRNRVYC AQSSSAAVDE SKNITMGDSF
IRPHLRQLAA YQPILPFEVL SAQLGRKPED IVKLDANENP YGPPPEVFEA LGNMKFPYVY
PDPQSRRLRD ALAQDSGLES EYILVGCGAD ELIDLIMRCV LDPGEKIIDC PPTFSMYVFD
AAVNGAGVIK VPRNPDFSLN VDRIAEVVEL EKPKCIFLTS PNNPDGSIIS EDDLLKILEM
PILVVLDEAY IEFSGVESRM KWVKKYENLI VLRTFSKRAG LAGLRVGYGA FPLSIIEYLW
RAKQPYNVSV AGEVAALAAL SNGKYLEDVR DALVRERERL FGLLKEVPFL NPYPSYSNFI
LCEVTSGMDA KKLKEDLAKM GVMVRHYNSQ ELKGYVRVSA GKPEHTDVLM ECLKQFY
