ID A0A1U8J9P2_GOSHI Unreviewed; 430 AA.
AC A0A1U8J9P2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN Name=LOC107905017 {ECO:0000313|RefSeq:XP_016687052.1,
GN ECO:0000313|RefSeq:XP_016687053.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016687052.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|EMBL:AUY62008.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TM-1_GhLMMD {ECO:0000313|EMBL:AUY62008.1}, and W0_GhLMMD
RC {ECO:0000313|EMBL:AUY62010.1};
RA Chai Q.;
RT "Transcriptome sequencing of wild type and lmm mutant cotton.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_016687052.1, ECO:0000313|RefSeq:XP_016687053.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016687052.1,
RC ECO:0000313|RefSeq:XP_016687053.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 ECO:0000256|RuleBase:RU000515};
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|RuleBase:RU000515}.
CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000256|ARBA:ARBA00008055,
CC ECO:0000256|RuleBase:RU004161}.
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DR EMBL; KY652848; AUY62008.1; -; mRNA.
DR EMBL; KY652850; AUY62010.1; -; mRNA.
DR RefSeq; XP_016687052.1; XM_016831563.1.
DR RefSeq; XP_016687053.1; XM_016831564.1.
DR STRING; 3635.A0A1U8J9P2; -.
DR PaxDb; 3635-A0A1U8J9P2; -.
DR GeneID; 107905017; -.
DR KEGG; ghi:107905017; -.
DR OMA; YQMDYAN; -.
DR OrthoDB; 2782182at2759; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000189702; Chromosome 19.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04823; ALAD_PBGS_aspartate_rich; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR030656; ALAD_AS.
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 PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000515};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515};
KW Reference proteome {ECO:0000313|Proteomes:UP000189702}.
SQ SEQUENCE 430 AA; 47124 MW; 8051DF3AB990B191 CRC64;
MASTIVNAPC TVPSVKGFET QNYVGLRPIS SLRFNSGRTS TSGRSRGLFV VRACERHDGH
VKKIEMSIEE CEAAVVAGNA PEAPPVPPKP AAPVGTPVIK PYQLTRRPRR NRKSPALRAS
FQETSISPAN FVYPLFIHEG QEDTPIGAMP GCYRLGWRHG LVEEVAKARD VGVNSIVLFP
KVPDALKSPT GDEAYNDNGL VPRTIRLLKD KFPDLVIYTD VALDPYSSDG HDGIVREDGV
IMNDETVHQL CKQAVSQARA GADVVSPSDM MDGRVGAIRA ALDSEGFHHV SIMSYTAKYA
SSFYGPFREA LDSNPRFGDK KTYQMNPANY REALVEAHED EAEGADILLV KPGLPYLDII
RLLRDQSPLP IAAYQVSGEY SMIKAGGVLK MIDEERVMME SLMCLRRAGA DIILTYFALQ
AARSLCGEKR
//
