HEM1_RHOCB
ID HEM1_RHOCB Reviewed; 409 AA.
AC P18079; D5AT85;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=RCAP_rcc01447;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2381418; DOI=10.1007/bf00259402;
RA Hornberger U., Liebetanz R., Tichy H.V., Drews G.;
RT "Cloning and sequencing of the hemA gene of Rhodobacter capsulatus and
RT isolation of a delta-aminolevulinic acid-dependent mutant strain.";
RL Mol. Gen. Genet. 221:371-378(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=1904045; DOI=10.1016/0378-1097(91)90181-9;
RA Wright M.S., Eckert J.J., Biel S.W., Biel A.J.;
RT "Use of a lacZ fusion to study transcriptional regulation of the
RT Rhodobacter capsulatus hemA gene.";
RL FEMS Microbiol. Lett. 62:339-342(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-401, SUBUNIT, COFACTOR-BINDING
RP SITES, SUBSTRATE-BINDING SITES, AND ACTIVE SITE.
RX PubMed=16121195; DOI=10.1038/sj.emboj.7600792;
RA Astner I., Schulze J.O., van den Heuvel J., Jahn D., Schubert W.D.,
RA Heinz D.W.;
RT "Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme
RT biosynthesis, and its link to XLSA in humans.";
RL EMBO J. 24:3166-3177(2005).
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:0000269|PubMed:16121195};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16121195}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X53309; CAA37393.1; -; Genomic_DNA.
DR EMBL; X53864; CAA37857.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85192.1; -; Genomic_DNA.
DR PIR; S10528; S10528.
DR RefSeq; WP_013067171.1; NC_014034.1.
DR PDB; 2BWN; X-ray; 2.10 A; A/B/D/E=1-401.
DR PDB; 2BWO; X-ray; 2.80 A; A/B/D/E=1-401.
DR PDB; 2BWP; X-ray; 2.70 A; A/B/D/E=1-401.
DR PDBsum; 2BWN; -.
DR PDBsum; 2BWO; -.
DR PDBsum; 2BWP; -.
DR AlphaFoldDB; P18079; -.
DR SMR; P18079; -.
DR STRING; 272942.RCAP_rcc01447; -.
DR PRIDE; P18079; -.
DR EnsemblBacteria; ADE85192; ADE85192; RCAP_rcc01447.
DR GeneID; 31490330; -.
DR KEGG; rcp:RCAP_rcc01447; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_1_5; -.
DR OMA; HRIDIFN; -.
DR OrthoDB; 479874at2; -.
DR BRENDA; 2.3.1.37; 5381.
DR UniPathway; UPA00251; UER00375.
DR EvolutionaryTrace; P18079; -.
DR Proteomes; UP000002361; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Heme biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..409
FT /note="5-aminolevulinate synthase"
FT /id="PRO_0000163828"
FT ACT_SITE 248
FT /evidence="ECO:0000269|PubMed:16121195"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16121195"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16121195"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16121195"
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:0000269|PubMed:16121195"
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:0000269|PubMed:16121195"
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:0000269|PubMed:16121195"
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:0000269|PubMed:16121195"
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:0000269|PubMed:16121195"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16121195"
FT MOD_RES 248
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> L (in Ref. 1; CAA37857 and 2; CAA37393)"
FT /evidence="ECO:0000305"
FT CONFLICT 402..409
FT /note="Missing (in Ref. 1; CAA37857 and 2; CAA37393)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:2BWN"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:2BWN"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 197..207
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2BWN"
FT TURN 216..221
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 298..321
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:2BWN"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:2BWN"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:2BWN"
FT HELIX 383..396
FT /evidence="ECO:0007829|PDB:2BWN"
SQ SEQUENCE 409 AA; 44374 MW; FCC89DA6EBA8DFB3 CRC64;
MDYNLALDKA IQKLHDEGRY RTFIDIEREK GAFPKAQWNR PDGGKQDITV WCGNDYLGMG
QHPVVLAAMH EALEAVGAGS GGTRNISGTT AYHRRLEAEI ADLHGKEAAL VFSSAYIAND
ATLSTLRVLF PGLIIYSDSL NHASMIEGIK RNAGPKRIFR HNDVAHLREL IAADDPAAPK
LIAFESVYSM DGDFGPIKEI CDIADEFGAL TYIDEVHAVG MYGPRGAGVA ERDGLMHRID
IFNGTLAKAY GVFGGYIAAS AKMVDAVRSY APGFIFSTSL PPAIAAGAQA SIAFLKTAEG
QKLRDAQQMH AKVLKMRLKA LGMPIIDHGS HIVPVVIGDP VHTKAVSDML LSDYGVYVQP
INFPTVPRGT ERLRFTPSPV HDLKQIDGLV HAMDLLWARC ALNRAEASA
