ID F3UVA7_STRSA Unreviewed; 323 AA.
AC F3UVA7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|ARBA:ARBA00020771};
DE EC=4.2.1.24 {ECO:0000256|ARBA:ARBA00012053};
DE AltName: Full=Porphobilinogen synthase {ECO:0000256|ARBA:ARBA00032837};
GN Name=hemB {ECO:0000313|EMBL:EGJ41075.1};
GN ORFNames=HMPREF9380_0450 {ECO:0000313|EMBL:EGJ41075.1};
OS Streptococcus sanguinis SK49.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888808 {ECO:0000313|EMBL:EGJ41075.1, ECO:0000313|Proteomes:UP000006459};
RN [1] {ECO:0000313|EMBL:EGJ41075.1, ECO:0000313|Proteomes:UP000006459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK49 {ECO:0000313|EMBL:EGJ41075.1,
RC ECO:0000313|Proteomes:UP000006459};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles.
CC Binds two molecules of 5-aminolevulinate per subunit, each at a
CC distinct site, and catalyzes their condensation to form
CC porphobilinogen. {ECO:0000256|ARBA:ARBA00025628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen;
CC Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00001227};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004694}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC ECO:0000256|RuleBase:RU004161}.
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:EGJ41075.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFFO01000003; EGJ41075.1; -; Genomic_DNA.
DR RefSeq; WP_002932272.1; NZ_GL890985.1.
DR AlphaFoldDB; F3UVA7; -.
DR PATRIC; fig|888808.3.peg.437; -.
DR eggNOG; COG0113; Bacteria.
DR HOGENOM; CLU_035731_0_0_9; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000006459; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00384; ALAD_PBGS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR013785; Aldolase_TIM.
DR PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR PANTHER; PTHR11458:SF0; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR Pfam; PF00490; ALAD; 1.
DR PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EGJ41075.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001415-5};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001415-3};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT ACT_SITE 193
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT ACT_SITE 246
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-1"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-3"
FT BINDING 203
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 215
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-5"
FT BINDING 272
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
FT BINDING 311
FT /ligand="5-aminolevulinate"
FT /ligand_id="ChEBI:CHEBI:356416"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001415-2"
SQ SEQUENCE 323 AA; 35702 MW; 2CBBD1E768F97306 CRC64;
MEFYRHRRLR RSSGLRQLVR ETKLSVDDFI QPLFVKEGLT EKKEVASMPG VYQFSLEDLL
PEVQECVDLG IRAFIVFGIP SGKDEIGSQA SAENGIVQEA IRLIKKHFPE TVVIADTCLC
EFTSHGHCGI LRGEEVDNDL SLTRLTEVAV SQARAGADVI APSNAMDGFV AAIRQGLDVA
GFEDIPIMSY AIKFASSFYG PFRDAGESAP AFGDRKTYQM NPANRLEALR EAKSDEEQGA
DFLMVKPALA FLDILRELRQ ETRLPLVTYN VSGEYAMVKA AAQQGWINEK AIVMETLTSM
KRAGADLIIT YFAKDAAGYL KEG
//
