HEM1_PARDP
ID HEM1_PARDP Reviewed; 409 AA.
AC P43089; A1B325;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=5-aminolevulinate synthase;
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=hemA; OrderedLocusNames=Pden_1822;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7928952; DOI=10.1128/jb.176.19.5919-5928.1994;
RA Page M.D., Ferguson S.J.;
RT "Differential reduction in soluble and membrane-bound c-type cytochrome
RT contents in a Paracoccus denitrificans mutant partially deficient in 5-
RT aminolevulinate synthase activity.";
RL J. Bacteriol. 176:5919-5928(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) 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 -!- SEQUENCE CAUTION:
CC Sequence=ABL69919.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U12508; AAA62279.1; -; Genomic_DNA.
DR EMBL; CP000489; ABL69919.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041529892.1; NC_008686.1.
DR AlphaFoldDB; P43089; -.
DR SMR; P43089; -.
DR STRING; 318586.Pden_1822; -.
DR PRIDE; P43089; -.
DR EnsemblBacteria; ABL69919; ABL69919; Pden_1822.
DR KEGG; pde:Pden_1822; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_1_5; -.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000000361; Chromosome 1.
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..409
FT /note="5-aminolevulinate synthase"
FT /id="PRO_0000163826"
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 156
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 365
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"
FT CONFLICT 35
FT /note="Q -> T (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="S -> A (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="A -> V (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..155
FT /note="FDGA -> STAP (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="A -> G (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="G -> A (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> E (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="G -> A (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..260
FT /note="AAS -> GFG (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> V (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 302..303
FT /note="LL -> FV (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..313
FT /note="ARI -> GRL (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="L -> A (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="I -> V (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="G -> S (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="P -> A (in Ref. 1; AAA62279)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 44560 MW; 1A2EEE178D58B32E CRC64;
MDYSAALDQA IGKLHEEGRY RTFIDIERRK GAYPQAVWTR PDGTETRITV WCGNDYLGMG
QHPVVLAAMH EALDATGAGS GGTRNISGTT VYHKRLEAEL SDLHGKEAAL VFSSAYIAND
ATLSTLRKLF PGLIIYSDEL NHASMIEGIK RFDGAKRIFR HNDVAHLREL LAADDPEAPK
LIAFESIYSM DGDFGPIKAI CDLADEFNAL TYLDEVHAVG MYGPRGGGVA ERDGLSHRID
IFNGTLGKAF GVFGGYIAAS ARMVDAIRSY APGFIFTTSL PPAVAAGAAA SIAFLKTAEG
QLLRDQQQLN ARILKMRLRG LGMPIMDHGS HIVPVHVGNP VHCKALSDML LADFGIYVQP
INFPTVPRGT ERLRFTPSPV HDPKQIDHLV KAMDSLWSQC KLNRSTSAA
