GSA_HISS2
ID GSA_HISS2 Reviewed; 432 AA.
AC B0UST3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 82.
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}; OrderedLocusNames=HSM_0850;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) 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: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}.
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DR EMBL; CP000947; ACA32524.1; -; Genomic_DNA.
DR RefSeq; WP_012341659.1; NC_010519.1.
DR AlphaFoldDB; B0UST3; -.
DR SMR; B0UST3; -.
DR STRING; 228400.HSM_0850; -.
DR EnsemblBacteria; ACA32524; ACA32524; HSM_0850.
DR KEGG; hsm:HSM_0850; -.
DR HOGENOM; CLU_016922_1_5_6; -.
DR OMA; WGPLIFG; -.
DR OrthoDB; 493793at2; -.
DR UniPathway; UPA00251; UER00317.
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 3: Inferred from homology;
KW Cytoplasm; Isomerase; Porphyrin biosynthesis; Pyridoxal phosphate.
FT CHAIN 1..432
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_1000121893"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00375"
SQ SEQUENCE 432 AA; 46703 MW; A6555726DFAEFF78 CRC64;
MTTSATLFYR AQQVIPGGVN SPVRAFKGVG GTPVFIEKAN GAYIFDIEGK QYIDYVGSWG
PMILGHNHPS ILSAVLKIAE NGLSFGTPTP LEIELAELIC QLVPSIEMVR MVNSGTEATM
SAIRLARGYT KRDKILKFEG CYHGHSDSLL VKAGSGSLTL GQPSSPGVPE DFAKHTITCE
YNNLQSVKNA FEQYPDQIAC VIVEPVAGNM NCILPKQDFL QGLRQLCNEY GSLFIIDEVM
TGFRVALGGA QSYYEVTPDL TTLGKVIGGG MPVGAFGGKK EIMQYIAPTG PVYQAGTLSG
NPIAMSAGIA CLNELKKEGN EQRLAMLTKK LALGLKNLAN QHNIPLVVNY VGGMFGIFFT
TQNEVTSYQQ AIQCDIERFN LFFHKMLEQG VYLAPSAFEA GFMSLAHTDA DIDRTLQAAD
IAFASLRSSS FS