HEM0_CERS4
ID HEM0_CERS4 Reviewed; 407 AA.
AC Q06965; Q3IXU1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=5-aminolevulinate synthase 2;
DE EC=2.3.1.37;
DE AltName: Full=5-aminolevulinic acid synthase;
DE AltName: Full=Delta-ALA synthase;
DE AltName: Full=Delta-aminolevulinate synthase;
GN Name=hemT; OrderedLocusNames=RHOS4_30750; ORFNames=RSP_3028;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8468290; DOI=10.1128/jb.175.8.2292-2303.1993;
RA Neidle E.L., Kaplan S.;
RT "Expression of the Rhodobacter sphaeroides hemA and hemT genes, encoding
RT two 5-aminolevulinic acid synthase isozymes.";
RL J. Bacteriol. 175:2292-2303(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA;
CC Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:356416; EC=2.3.1.37;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P18079};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P18079}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: Expressed in the mutant strain HemA1 but expression in the
CC wild-type strain has not been proven. {ECO:0000305}.
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DR EMBL; L07489; AAA26124.1; -; Genomic_DNA.
DR EMBL; CP000144; ABA80643.1; -; Genomic_DNA.
DR PIR; A49845; A49845.
DR RefSeq; WP_011338981.1; NZ_CP030272.1.
DR RefSeq; YP_354544.1; NC_007494.2.
DR AlphaFoldDB; Q06965; -.
DR SMR; Q06965; -.
DR STRING; 272943.RSP_3028; -.
DR EnsemblBacteria; ABA80643; ABA80643; RSP_3028.
DR KEGG; rsp:RSP_3028; -.
DR PATRIC; fig|272943.9.peg.3445; -.
DR eggNOG; COG0156; Bacteria.
DR OMA; RSQMFAK; -.
DR PhylomeDB; Q06965; -.
DR BioCyc; MetaCyc:MON-13234; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000002703; Chromosome 2.
DR GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01821; 5aminolev_synth; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Heme biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..407
FT /note="5-aminolevulinate synthase 2"
FT /id="PRO_0000163830"
FT ACT_SITE 248
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 189
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 217
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 245
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 277
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 278
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18079"
FT MOD_RES 248
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P18079"
SQ SEQUENCE 407 AA; 44333 MW; 4772E3EC1DA55D82 CRC64;
MEFSQHFQKL IDDMRLDGRY RTFAELERIA GEFPTALWHG PDGQARRVTV WCSNDYLGMG
QNAEVLAAMH RSIDLSGAGT GGTRNISGTN RQHVALEAEL ADLHGKESAL IFTSGWISNL
AALGTLGKIL PECAIFSDAL NHNSMIEGIR RSGAERFIFH HNDPVHLDRL LSSVDPARPK
IVAFESVYSM DGDIAPIAEI CDVAERHGAL TYLDEVHAVG LYGPRGGGIS DRDGLADRVT
IIEGTLAKAF GVMGGYVSGP SLLMDVIRSM SDSFIFTTSI CPHLAAGALA AVRHVKAHPD
ERRRQAENAV RLKVLLQKAG LPVLDTPSHI LPVMVGEAHL CRSISEALLA RHAIYVQPIN
YPTVARGQER FRLTPTPFHT TSHMEALVEA LLAVGRDLGW AMSRRAA
