GSA_YERPE
ID GSA_YERPE Reviewed; 426 AA.
AC Q8ZBL9; Q0WBQ7;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA {ECO:0000255|HAMAP-Rule:MF_00375};
DE EC=5.4.3.8 {ECO:0000255|HAMAP-Rule:MF_00375};
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000255|HAMAP-Rule:MF_00375};
DE Short=GSA-AT {ECO:0000255|HAMAP-Rule:MF_00375};
GN Name=hemL {ECO:0000255|HAMAP-Rule:MF_00375};
GN OrderedLocusNames=YPO3389, y0799, YP_0296;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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:0000255|HAMAP-Rule:MF_00375};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00375};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_00375}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00375}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00375}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL590842; CAL21978.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84386.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS60571.1; -; Genomic_DNA.
DR PIR; AG0411; AG0411.
DR RefSeq; WP_002209362.1; NZ_WUCM01000008.1.
DR RefSeq; YP_002348281.1; NC_003143.1.
DR PDB; 4E77; X-ray; 2.00 A; A=1-426.
DR PDBsum; 4E77; -.
DR AlphaFoldDB; Q8ZBL9; -.
DR SMR; Q8ZBL9; -.
DR IntAct; Q8ZBL9; 1.
DR STRING; 214092.YPO3389; -.
DR PaxDb; Q8ZBL9; -.
DR DNASU; 1145746; -.
DR EnsemblBacteria; AAM84386; AAM84386; y0799.
DR EnsemblBacteria; AAS60571; AAS60571; YP_0296.
DR GeneID; 57975320; -.
DR KEGG; ype:YPO3389; -.
DR KEGG; ypk:y0799; -.
DR KEGG; ypm:YP_0296; -.
DR PATRIC; fig|214092.21.peg.3871; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_6; -.
DR OMA; WGPLIFG; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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; Cytoplasm; Isomerase; Porphyrin biosynthesis;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..426
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000120474"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:4E77"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:4E77"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4E77"
FT TURN 239..244
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:4E77"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 302..315
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 320..341
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:4E77"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 368..372
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:4E77"
FT HELIX 409..423
FT /evidence="ECO:0007829|PDB:4E77"
SQ SEQUENCE 426 AA; 45794 MW; 1BB579AE82D49BA4 CRC64;
MSKSENLYAQ AQQLIPGGVN SPVRAFTGVG GIPLFIERAD GAYLFDVDGK AYIDYVGSWG
PMILGHNHPA IRQAVIEAVE RGLSFGAPTE MEVKMAQLVT DLVPTMDMVR MVNSGTEATM
SAIRLARGYT GRDKIIKFEG CYHGHADCLL VKAGSGALTL GQPNSPGVPT DFAKHTLTCT
YNDLASVRQA FEQYPQEVAC IIVEPVAGNM NCIPPLPEFL PGLRALCDEF GALLIIDEVM
TGFRVALAGA QDYYHVIPDL TCLGKIIGGG MPVGAFGGRR EVMNALAPTG PVYQAGTLSG
NPIAMAAGFA CLTEISQVGV YETLTELTDS LATGLRHAAK EENIPLVVNH VGGMFGLFFT
NADTVTCYQD VMNCDVERFK RFFHLMLEEG VYLAPSAFEA GFMSLAHSNE DIQKTVNAAR
RCFAKL
