GSA1_ARATH
ID GSA1_ARATH Reviewed; 474 AA.
AC P42799;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase 1, chloroplastic {ECO:0000303|PubMed:7908550};
DE Short=AtGSA1 {ECO:0000303|PubMed:27303897};
DE Short=GSA 1 {ECO:0000303|PubMed:7908550};
DE EC=5.4.3.8 {ECO:0000269|PubMed:7908550};
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase 1 {ECO:0000303|PubMed:7908550};
DE Short=GSA-AT 1 {ECO:0000303|PubMed:7908550};
DE Flags: Precursor;
GN Name=GSA1 {ECO:0000303|PubMed:7908550};
GN Synonyms=HEML1 {ECO:0000303|PubMed:15951223};
GN OrderedLocusNames=At5g63570 {ECO:0000312|Araport:AT5G63570};
GN ORFNames=MBK5.3 {ECO:0000312|EMBL:BAB10450.1};
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 [GENOMIC DNA], FUNCTION, INDUCTION BY LIGHT, TISSUE
RP SPECIFICITY, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7908550; DOI=10.2307/3869644;
RA Ilag L.L., Kumar A.M., Soell D.;
RT "Light regulation of chlorophyll biosynthesis at the level of 5-
RT aminolevulinate formation in Arabidopsis.";
RL Plant Cell 6:265-275(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP REVIEW.
RX PubMed=15951223; DOI=10.1016/j.tplants.2005.05.005;
RA Beale S.I.;
RT "Green genes gleaned.";
RL Trends Plant Sci. 10:309-312(2005).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=25840087; DOI=10.1093/pcp/pcv050;
RA Toyokura K., Yamaguchi K., Shigenobu S., Fukaki H., Tatematsu K., Okada K.;
RT "Mutations in plastidial 5-aminolevulinic acid biosynthesis genes suppress
RT a pleiotropic defect in shoot development of a mitochondrial GABA shunt
RT mutant in Arabidopsis.";
RL Plant Cell Physiol. 56:1229-1238(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 41-474, N6-(PYRIDOXAL
RP PHOSPHATE)LYSINE, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27303897; DOI=10.1107/s2053230x16007263;
RA Song Y., Pu H., Jiang T., Zhang L., Ouyang M.;
RT "Crystal structure of glutamate-1-semialdehyde-2,1-aminomutase from
RT Arabidopsis thaliana.";
RL Acta Crystallogr. F 72:448-456(2016).
CC -!- FUNCTION: Transaminase converting glutamate 1-semialdehyde (GSA) to 5-
CC aminolevulinate (ALA). Involved in the biosynthesis of tetrapyrroles.
CC {ECO:0000269|PubMed:7908550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate;
CC Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416;
CC EC=5.4.3.8; Evidence={ECO:0000269|PubMed:7908550};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:27303897};
CC Note=Can use both pyridoxamine 5'-phosphate (PMP) and pyridoxal 5'-
CC phosphate (PLP) as cofactors. {ECO:0000269|PubMed:27303897};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=338 nm;
CC Note=A relatively lower peak at 418 nm is also observed. At pH 7.5.
CC {ECO:0000269|PubMed:27303897};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC {ECO:0000269|PubMed:7908550}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis. {ECO:0000269|PubMed:7908550}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27303897}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q42522}.
CC -!- TISSUE SPECIFICITY: Present in all tissues tested.
CC {ECO:0000269|PubMed:7908550}.
CC -!- INDUCTION: By light. In etiolated seedlings, initial expression is
CC reduced but after further illumination, levels steadily increase.
CC {ECO:0000269|PubMed:7908550}.
CC -!- DISRUPTION PHENOTYPE: Suppresses partially the ENF1 disruption
CC pleiotropic developmental phenotypes. {ECO:0000269|PubMed:25840087}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR EMBL; U03773; AAA19117.1; -; Genomic_DNA.
DR EMBL; AB005234; BAB10450.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97770.1; -; Genomic_DNA.
DR EMBL; AY102109; AAM26679.1; -; mRNA.
DR EMBL; AY139804; AAM98110.1; -; mRNA.
DR RefSeq; NP_201162.1; NM_125752.4.
DR PDB; 5HDM; X-ray; 1.25 A; A/B=41-474.
DR PDBsum; 5HDM; -.
DR AlphaFoldDB; P42799; -.
DR SMR; P42799; -.
DR BioGRID; 21718; 17.
DR IntAct; P42799; 1.
DR STRING; 3702.AT5G63570.1; -.
DR PaxDb; P42799; -.
DR PRIDE; P42799; -.
DR ProteomicsDB; 222368; -.
DR EnsemblPlants; AT5G63570.1; AT5G63570.1; AT5G63570.
DR GeneID; 836476; -.
DR Gramene; AT5G63570.1; AT5G63570.1; AT5G63570.
DR KEGG; ath:AT5G63570; -.
DR Araport; AT5G63570; -.
DR TAIR; locus:2160554; AT5G63570.
DR eggNOG; KOG1401; Eukaryota.
DR HOGENOM; CLU_016922_1_5_1; -.
DR InParanoid; P42799; -.
DR OrthoDB; 1160614at2759; -.
DR PhylomeDB; P42799; -.
DR BioCyc; ARA:AT5G63570-MON; -.
DR BioCyc; MetaCyc:AT5G63570-MON; -.
DR BRENDA; 5.4.3.8; 399.
DR UniPathway; UPA00251; UER00317.
DR UniPathway; UPA00668; -.
DR PRO; PR:P42799; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42799; baseline and differential.
DR Genevisible; P42799; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00713; hemL; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll biosynthesis; Chloroplast; Isomerase; Plastid;
KW Porphyrin biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..474
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase 1,
FT chloroplastic"
FT /id="PRO_0000001255"
FT MOD_RES 314
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:27303897,
FT ECO:0007744|PDB:5HDM"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:5HDM"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5HDM"
FT TURN 109..113
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 164..179
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:5HDM"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:5HDM"
FT TURN 288..293
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:5HDM"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 351..364
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 369..390
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:5HDM"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 424..436
FT /evidence="ECO:0007829|PDB:5HDM"
FT HELIX 457..471
FT /evidence="ECO:0007829|PDB:5HDM"
SQ SEQUENCE 474 AA; 50370 MW; 0D5E1A84F2B7433E CRC64;
MSATLTGSGT ALGFSCSSKI SKRVSSSPAS NRCCIKMSVS VDEKKKSFSL QKSEEAFNAA
KNLMPGGVNS PVRAFKSVGG QPVLIDSVKG SKMWDIDGNE YIDYVGSWGP AIIGHADDEV
LAALAETMKK GTSFGAPCLL ENVLAEMVIS AVPSIEMVRF VNSGTEACMG VLRLARAFTN
KEKFIKFEGC YHGHANAFLV KAGSGVATLG LPDSPGVPKA ATSDTLTAPY NDLEAVEKLF
AAHKGEISAV ILEPVVGNSG FIPPTPEFIN GLRQLTKDNG VLLIFDEVMT GFRLAYGGAQ
EYFGITPDLT TLGKIIGGGL PVGAYGGRRD IMEMVAPAGP MYQAGTLSGN PLAMTAGIHT
LKRLKQAGTY EYLDKITKEL TNGILEAGKK TGHPMCGGYI SGMFGFFFAE GPVYNFADSK
KSDTEKFGRF FRGMLEEGVY FAPSQFEAGF TSLAHTPEDI QLTIAAAERV LSRI
