GSA_PSEAE
ID GSA_PSEAE Reviewed; 427 AA.
AC P48247;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
DE Short=GSA;
DE EC=5.4.3.8;
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE Short=GSA-AT;
GN Name=hemL; OrderedLocusNames=PA3977;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7565600; DOI=10.1007/bf02191605;
RA Hungerer C., Troup B., Romling U., Jahn D.;
RT "Cloning, mapping and characterization of the Pseudomonas aeruginosa hemL
RT gene.";
RL Mol. Gen. Genet. 248:375-380(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily. {ECO:0000305}.
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DR EMBL; X82072; CAA57575.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07364.1; -; Genomic_DNA.
DR PIR; G83149; G83149.
DR PIR; S57898; S57898.
DR RefSeq; NP_252666.1; NC_002516.2.
DR RefSeq; WP_003093150.1; NZ_QZGE01000001.1.
DR PDB; 5I92; X-ray; 1.75 A; A/B/C/D/E/F=1-427.
DR PDBsum; 5I92; -.
DR AlphaFoldDB; P48247; -.
DR SMR; P48247; -.
DR STRING; 287.DR97_3888; -.
DR PaxDb; P48247; -.
DR PRIDE; P48247; -.
DR EnsemblBacteria; AAG07364; AAG07364; PA3977.
DR GeneID; 880859; -.
DR KEGG; pae:PA3977; -.
DR PATRIC; fig|208964.12.peg.4169; -.
DR PseudoCAP; PA3977; -.
DR HOGENOM; CLU_016922_1_5_6; -.
DR InParanoid; P48247; -.
DR OMA; WGPLIFG; -.
DR PhylomeDB; P48247; -.
DR BioCyc; PAER208964:G1FZ6-4051-MON; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000002438; 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..427
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000120433"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 157
FT /note="A -> S (in Ref. 1; CAA57575)"
FT /evidence="ECO:0000305"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:5I92"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:5I92"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:5I92"
FT TURN 239..244
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:5I92"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 320..341
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:5I92"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:5I92"
FT HELIX 409..424
FT /evidence="ECO:0007829|PDB:5I92"
SQ SEQUENCE 427 AA; 45398 MW; 670EB87D144E2D28 CRC64;
MSRSETLFNN AQKHIPGGVN SPVRAFKSVG GTPLFFKHAE GAYVLDEDDK RYVDYVGSWG
PMILGHSHPD VLDAVRRQLD HGLSYGAPTA LEVEMADLVC SMVPSMEMVR MVSSGTEATM
SAIRLARGYT GRDSIIKFEG CYHGHSDSLL VKAGSGALTF GVPNSPGVPA AFAKHTLTLP
FNDIEAVRKT LGEVGKEVAC IIVEPVAGNM NCVPPAPGFL EGLREACDEH GVVLIFDEVM
TGFRVALGGA QAYYGVTPDL STFGKIIGGG MPVGAFGGKR EIMQQISPLG PVYQAGTLSG
NPLAMAAGLT TLRLISRPGF HDELTAYTTR MLDGLQQRAD AAGIPFVTTQ AGGMFGLYFS
GADAIVTFED VMASDVERFK RFFHLMLDGG VYLAPSAFEA GFTSIAHGDK ELEITLNAAE
KAFAALK