ID A0A1Q9DPX4_SYMMI Unreviewed; 2150 AA.
AC A0A1Q9DPX4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN Name=HEMB {ECO:0000313|EMBL:OLP97230.1};
GN ORFNames=AK812_SmicGene20473 {ECO:0000313|EMBL:OLP97230.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP97230.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP97230.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP97230.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) 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 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OLP97230.1}.
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DR EMBL; LSRX01000442; OLP97230.1; -; Genomic_DNA.
DR OrthoDB; 2782182at2759; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; cd06257; DnaJ; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR030656; ALAD_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR019537; TMEM65.
DR PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR PANTHER; PTHR11458:SF0; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR Pfam; PF00490; ALAD; 2.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF10507; TMEM65; 1.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF51569; Aldolase; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000515};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 379..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..146
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REPEAT 1138..1170
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1173..1196
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1243..1268
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2150 AA; 234065 MW; A6CC8C9E288F6E28 CRC64;
MTQDDIQVAS ESESRAEESV EEASIEAEEA PIQKTSSAWQ NHDDVEWTAD DEDEWQKDTH
RDYYEALGLT RSDGMSISAS RVRAAYHRMV QKWHPDFQSI ETSGSCDQEN GPQRTQHEVL
RRFWLITEAY LVLKDPERRR IYDECGFAHF KQSEACYQEP VFEQARRSAP KVALGSQTHL
QLVVCRTSAA EMNALPRSVR TTAHKINYGI DLRISTISFL TPQRHGTRWP TGNVVGNFTG
TVGSCGGPAL LWWRALCPSQ KGCFWMRNTQ PDFHDYGPKN QEARPSVTNL RRHFIVCAVP
MVGFGIMDNT IMIHAGEMID EHLGMALGLS TMASAAAGQV ISDFSGVCFG GTLEAAASKL
GLRHPALSDK QRQMSVVKLL GTAGSAIGVL CGCLLGMLNL LFLDLRKVER QKKHAELQTI
CKTFAVDGPA HFEAERCTLY IRDSDDKYLW TFAKRWQLSD AQLSEFKSFT EEQDYSDGAI
ASALAELHFK ASEIAHLVRK SKEVSSDEFR VYLEQQLERP TKIKLRAGGT KKYVVDAKKL
LNTPVVYSDP RFAATHRNTG SGTRACSVLV CPILSKRSGE VLGVLEVINK MPKRLQKPVF
TEMDEKLALM MCSHVASIVD TICDEDAYQV YEDFFNGTDP EARDFLLMNG GVADSGSESD
DSMEGELAVE PGDSRAGRQA EADGPQLPPE MAKAVGEASS VDQFRTMLNG VLSTTLRRDS
GEKECRPHTA QAKGLERQRR RSAKKARAPV KPRMQAWKCW RGARHIRQVC NKRREGGNRR
PAAEKEPACQ NSLPSCQMTA EVRPVASPGS QLFCFLGGAQ EPETIVQCNK MTGDSRVVAV
GAVAATVACT AFVGTAPSQG PGSARALRAG AAAAAVPARA SSTSPTAVAA AAAFAGFALA
ARGRQQHGKA KTLRHFFGEA ETETQVAEVT QVPVTQHPPG SRIPDGTPTP HPMAIRKRPR
RNRRLPAQRN MFSETRLTAA NFILPIFVHE GTEDIPISSM PDVSRVGVDT GLLREVEEAV
KLGVKSVVIF PKTPDELKTQ TAEECFNPAG LAQRAISNVK KAFPDVEATP RKREAALRAC
SKLACAQSLT DEHHVCSRLV RMKQAEMLLR LLSQASEGDC LHHLPQCTEK DINARTADGA
TALHYAASAG YADVCLELLE SPLFMQVNDQ DASGCTALHY AACKGHREVC RALLQHWRFS
AQDTQDWNGW TALHVAAAHG QPTTCSTLLE SPRFKVLTAR DKNGMTALHV ATARGRADVC
SALSDHGAFA GIAAVDNFGR TVHAMRKEPT LKDRGVQTIN VPKGVAKRTP STKAKPQMEK
WQSLAKWTSH LQKIQDEAPV VPTQSLEEEV VARLSQVAEL ETSLEGGSNV KDFAARGNED
TEAPHKLHSI DSRDSETHGA QAMAARPSSN APSTGKAFGN LSVARAEPEE DDRQFAARSG
DSSAADTHAT HAAGQVSDER TLSASAAAGE ATGHPTKVAT PTTSEGNKPA DGDLLESPKN
KQDSATVSAE VALDHEAGTT KVNTEDRNGP QDEPEDRSDS AQRPGAGTVS HESWQEETKM
VSDAEADLAK EEGNQVETYD NDERTVEKSN KVADENNTAA DAPKPGDEMD GTPQATEEQG
NGSAEGGRQK RNRQQRREKL KVRQLAGVDA EPPRTIRNKL KDVMKQEATD HQQPEAQTAD
GKAADAAEEA SKSEEEQEAR QAAETAALAQ EDEKSREVAR AEEERKIKEA AEAAARAEEE
RKAREAAEAA EAAARAEEER KAREAAEAAE AAARAEEERK AQEAAEAAEA AARAEEERKA
REAAEAAEAA ARAEEERKAR EAAEAAEAAA RAEEERKARE AAEAAEAAAR AEDDRKTLAA
EDEEAGRQAD DHHSSNEDED KVADATGGKE KKKKLKKPKQ NQGDAEPKKK GKKKKKDIIV
TVGQVTFAVV YTDVALDPYN SLGHDGIVRS DGVILNDETI AYLCKQAVSQ AEAGADYVSP
SDMMDGRIGA IRDALDEAGF TNVGIMAYSA KYASAFYGPF REALDSNPVI AEDWQVPKGK
ETYQQDPANY KEALLEAALD EEEGADILMV KPAMPYLDII KGLHEQSNLP IAAYHVSGEY
AMLKAAALNG WLDEKAVVLE ALLSIRRAGA TVILTYYAKQ AARWLQEEDA
//
