ID A0A0E0E626_9ORYZ Unreviewed; 2751 AA.
AC A0A0E0E626;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI06G26810.2};
RN [1] {ECO:0000313|EnsemblPlants:OMERI06G26810.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI06G26810.2};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI06G26810.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC specific tag for transcriptional activation.
CC {ECO:0000256|ARBA:ARBA00002581}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00000780};
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}.
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 STRING; 40149.A0A0E0E626; -.
DR EnsemblPlants; OMERI06G26810.2; OMERI06G26810.2; OMERI06G26810.
DR Gramene; OMERI06G26810.2; OMERI06G26810.2; OMERI06G26810.
DR eggNOG; KOG1778; Eukaryota.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000008021; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd04823; ALAD_PBGS_aspartate_rich; 1.
DR CDD; cd15614; PHD_HAC_like; 1.
DR Gene3D; 3.30.60.90; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR030656; ALAD_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013857; NADH-UbQ_OxRdtase-assoc_prot30.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00490; ALAD; 1.
DR Pfam; PF08547; CIA30; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF13460; NAD_binding_10; 2.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 2.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 597..678
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 1037..1472
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1354..1417
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1474..1532
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1533..1617
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1625..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2403..2432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2751 AA; 305585 MW; 79CE911202E3B018 CRC64;
MKQGQGAHLS GQRIGHHPTA QMNPGDGDGR QQVASGHASA DPELMNLAIW ELLSREPKLQ
TRPRKLVSDL AKRFEAVIYK KNPNKAAYYS ILNGEIFPHL QHALSTHMAQ HQQGQQMLQQ
LTSSSSYGTT IPIPDVVQNA SGNTRALYEM DNTGGPMSNR HHHFSANFPL HSTTKGASLE
MSAVSMQEGK ITHMIPTPGS SNQQSLPGNF HYSTGTGYLN GKSNVMAQMQ EQQAPFASKI
NCCPVQRDLG GYAGSGVHSD ILNNSSPYGV SEAHMIDGMG LHRSNVQVIN RTVVPETFIN
PSPYGISPNK PLQRHVNPST RSTPTPADIA ASTSFNGTGS SALSTTSYLD MTAVNSLPKS
RMDSGLIMSQ PTIQSFQTEH YIQTEGLDLQ EKISLEQLHQ QVNQLHLIQP HSQYVQNQCS
LKLQQQNSLH HLVMSRGNVL TQCHLGSDHA EKLLDKRNQL HSELVSSQIN EHVGLTNLQG
HYEQTQYHDN YKKGQMSASS QNLGIPAPHD LLPPQQQFDD GSYRLSCFLK ETYTKPLQPH
CKSKPMKEVT VTSLLSGKIQ DGFCQKKMAR DREHHPIISG WHSAGCAATS FGSEEVMENT
KQYHDQARWL LFLFHAKSCT SPPGSCKSSY CDRVRELVIH LTDCQIKDCP YRHCRESKMV
SDHYKNCINE HCHVCCKAKE MLRRSSELAH KQNPAEPILI TQHNMNQRSA DRVHGDRMDI
DQAVETFDDQ PPAAKRPKLQ LVSPDASENV PVCQKNPGFM LQEAHPRQLD QNKKMVPDQE
VDVGLDIRHP QVTLVSCHGS DEKIGAAQNT VIPGALNKIH CHVQQETVVA DKESVTVDVK
KKTGSVDVTI SKTGKPKVKG VSLMELFTPE QIHEHINSLR QWIGQSKAKA EKNQVIGYSE
SESLCQLCKV ENLTFEPRPI YCSPCGARIK RNASYYTGST AMGRLFFCIS CYNASLGNTI
EVELIKLSKA DLEKKRNSDE PEEGWVQCDK CECWQHQICA LFNARRNDVE EAEYTCFKCY
IEEFKRGLRM PLPESVVRGA KDLPRTMLSD HIEERLFKRL REERQERANK LKTSLDEVPG
ADGLVVRVVS SVDKKLEVKP RFFKILQEDN YPAEFPYKSK AILLFQKIEG VEVCLFGMYV
QEYGAECKFP NQRRVYLSYL DSVKYFRPDI ETVSGQALRT YVYHEILIGY LEYCKQRGFT
SCYIWACPPV KGEDYILYCH PEIQKTPKPD KLRQWYLSML QKAIKENIVV ELTNLYDQFF
VTAKECKIKV SAACLPYFDG DYWPGAAEDI INQLQLEGDG KLLKKGRVNK IITKRALKAA
GHTDLSGNAS KEAMLMQKLG EIICPIKDDL IMVHLQYSCS HCCTFMVSGR RWVCNECKSF
YICDRCYNAE QWLEEKERHP SNSKCLHILH PVEIVGVSED TKDRDIILEN EIFDTRQAFL
SFCQGYYYQY DTLRRAKHST MMMLYHLHNP TGPAFVATCN VCNCDIENGQ GWYCKDCPDF
DMCASCYQKH GGANHHHKLT NHPSSAECNV QNKGAWQKHV QQVRVWLELA LHASSCHVRN
CQYPNCRKLK GLFHHGAQCK IRLSKGCKQC ARMWYIIRLH SQSCRQSDCA VPRCRDFKSF
KRKQNQLSES RRMASVNERP QPEPITAATQ TSSPLYHRGR VVAQCNLATN FPPPQQHPSM
AAAIVAARAP PGGGGAAAVI AYHHCASPSR ALPLAAGPSA GGGVVVGRRY HHHHGGACCF
AAKPTQVAAE VDQEGAAEPG PGVASANAAA DVKPRKKARS RRGRKGKRSS SSSSSESSTT
AVLEEEEEEE KKAEEDGEEG KRKEKAAGLD LDEVMAVSPV GLGRRSRQIF DEVWRKFSRL
GQMSSASSTA LAEEEQAVLI RGGPMCEFTV PGAQDTTVLV VGATSRIGRI VVRKLMLRGY
NVKALVRRND AEVIDMLPRS VDIVVGDVGD PSTVKSAVSG CSKIIYCATA RSTITGDLNR
VDNQGVRNVS KAFQDYYNEL AQLRAGKSSK SKLLIAKFKS PKSLNGWEVD QGSYFPNTFA
SRFDEGIDAS FDFSEAGQAV FSGFVFTRGG YVEISKRLSL PLGSTLDRYD GLLFSVGGNG
RSYVVILETG PLADTSQSKK YFARMTTKVG FCRVRVPFSA FRPVNPQDPP LDPFLVHTLT
IRFEPKRQRP GDGSQSATDP RNFELILEYI KALPTGQETD FILVSCSGSG IEPNRREQVL
KAKKAGEDAL RRSGLGYTIV RPGPLQEEPG GQRALIFDQG NRISQGISCA DVADICVKAL
HDSTARNKSF DVCYEYVAEQ GNELYELVAH LPDKANNYLT PALSAMASTV SFSPANVQML
QGRSCHGHAA FGGCSAVPRT GPRMRSVAVR VSSEQEAAPA IRAPSGRTIE ECEADAVAGR
FLAPPPLVRP KAPEGTPQIR PLDLTKRPRR NRRSPALRAA FQETTISPAN LVLPLFIHEG
EDDAPIGAMP GCYRLGWRHG LLDEVYKSRD VGVNSFVLFP KVPDALKSQS GDEAYNDNGL
VPRTIRLLKD KFPDIVVYTD VALDPYSSDG HDGIVREDGV IMNDETVYQL CKQAVSQARA
GADVVSPSDM MDGRVGAIRA ALDAEGFHDV SIMSYTAKYA SSFYGPFREA LDSNPRFGDK
KTYQMNPANY REALLETAAD EAEGADILLV KPGLPYLDVI RLLRDNSALP IAAYQVSGEY
SMIKAGGALN MIDEEKVMME SLMCLRRAGA DIILTYFARQ AANVLCGMRS N
//
