ID Q1Z1B4_9GAMM Unreviewed; 432 AA.
AC Q1Z1B4;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|HAMAP-Rule:MF_00375};
DE Short=GSA {ECO:0000256|HAMAP-Rule:MF_00375};
DE EC=5.4.3.8 {ECO:0000256|HAMAP-Rule:MF_00375};
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|HAMAP-Rule:MF_00375};
DE Short=GSA-AT {ECO:0000256|HAMAP-Rule:MF_00375};
GN Name=hemL {ECO:0000256|HAMAP-Rule:MF_00375};
GN ORFNames=P3TCK_13540 {ECO:0000313|EMBL:EAS42282.1};
OS Photobacterium profundum 3TCK.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS42282.1, ECO:0000313|Proteomes:UP000003789};
RN [1] {ECO:0000313|EMBL:EAS42282.1, ECO:0000313|Proteomes:UP000003789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3TCK {ECO:0000313|EMBL:EAS42282.1,
RC ECO:0000313|Proteomes:UP000003789};
RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00375};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|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:0000256|ARBA:ARBA00004819}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily.
CC {ECO:0000256|ARBA:ARBA00008981, ECO:0000256|HAMAP-Rule:MF_00375}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAS42282.1}.
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DR EMBL; AAPH01000022; EAS42282.1; -; Genomic_DNA.
DR RefSeq; WP_006230605.1; NZ_CH724135.1.
DR AlphaFoldDB; Q1Z1B4; -.
DR HOGENOM; CLU_016922_1_5_6; -.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00251; UER00317.
DR Proteomes; UP000003789; Unassembled WGS sequence.
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:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00713; hemL; 1.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EAS42282.1};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00375};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW Rule:MF_00375};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00375}; Transferase {ECO:0000313|EMBL:EAS42282.1}.
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00375"
SQ SEQUENCE 432 AA; 46051 MW; 11AFD0A49CA54488 CRC64;
MSKSADLFAK AQEIIPGGVN SPVRAFAGVG GSPLFIERAD GAYIFDADGK AYIDYVGSWG
PMILGHNHVA VRDAVIKAAQ QGLSFGAPTE MEITMAELVS QLVPSMEQIR MVSSGTEATM
SAIRLARGFT NRDKIIKFEG CYHGHADCLL VKAGSGALTL GQPSSPGVPA DFAKHTLTCT
YNDLETVREA FAAHPEQIAC IIVEPVAGNM NCIPPVPGFL EGLRTICDEF GALLILDEVM
TGFRVSEGGA QGYYNIKPDL TTLGKIIGGG MPVGAFGGRK DVMQYVAPTG PVYQAGTLSG
NPVAMAAGYA CLSVLTEEGN EKRLANTTKI LANGFKALAD KYDIPLAINQ VGGMFGFFFT
EQETVTSYAD VTKCDIERFK RFFNLMLENG IYLAPSAYEA CFTSLAHRDK EIEATLNAAE
RAFATLAKEA NA
//
