ID G0SUF9_RHOT2 Unreviewed; 1758 AA.
AC G0SUF9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN ORFNames=RTG_00066 {ECO:0000313|EMBL:EGU13629.1};
OS Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS (Rhodotorula glutinis (strain ATCC 204091)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU13629.1, ECO:0000313|Proteomes:UP000006141};
RN [1] {ECO:0000313|EMBL:EGU13629.1, ECO:0000313|Proteomes:UP000006141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC {ECO:0000313|Proteomes:UP000006141};
RX PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA Lawrence M.L.;
RT "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT 204091.";
RL Genome Announc. 2:E0004614-E0004614(2014).
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}.
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:EGU13629.1}.
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DR EMBL; AEVR02000026; EGU13629.1; -; Genomic_DNA.
DR HOGENOM; CLU_239165_0_0_1; -.
DR InParanoid; G0SUF9; -.
DR UniPathway; UPA00251; UER00318.
DR Proteomes; UP000006141; 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; cd04824; eu_ALAD_PBGS_cysteine_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 InterPro; IPR021047; Mannosyltransferase_CMT1.
DR PANTHER; PTHR34144; CHROMOSOME 8, WHOLE GENOME SHOTGUN SEQUENCE; 1.
DR PANTHER; PTHR34144:SF7; CRYPTOCOCCAL MANNOSYLTRANSFERASE 1-DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00490; ALAD; 1.
DR Pfam; PF11735; CAP59_mtransfer; 2.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000515};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515};
KW Reference proteome {ECO:0000313|Proteomes:UP000006141};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 566..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1241..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 417..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1758 AA; 194140 MW; B23E4F289D4016CC CRC64;
MSDSLAVPIQ STLAGGYFHP LLRSLQAERH LTKDMLMYPI FITDEPDAVV EIKSLPGQKR
WGINKLHAFL APLVAKGLRS VILFGVPLHM QKDSRGSPAD DPNTPVILAT QLIRREFPGV
VVACDVCLCE YTDHGHCGEL CDVSTLTEAE QVAQAKVIDN GKSVKRMQEV ALAYARAGAQ
IVAPSDMMDG RIGAIKQALV DNGFGNRCSV MSYSAKFASG MYGPFREAAG SVPNFGDRKC
YQLPPNARGL ARRAIFRDVA EGADFLMVKP AMPYLDIMRE ARELAPNHPL ACYQVSGEFA
MLHAGAEAGV YELKTMAFES VEGFLRAGCT LVLTYFTPDF LDWLDEDKHL PSTPRHPSAR
FFRTKPSAEL SNEFLPCATH ACMHPSSRGA RCQHHRVTDA EVRTMVSLLS LFSTESNAAT
RSSPSSGNSV GCAPRTISNP PRSLSLSLLS PNYTVLQCAA LAMPALFRTA SPSPRSPPPS
STRDSLDSQA DTAETPLLPR WNTAKHSKDW EDSADEGRER SFLRPAGNGR TRADGRPYSH
ALDLPSSPRS YNATLRSHRR QARLVGLLYS SAWVCFAGTC LIGAGVLGWV GHFLWMRHAA
YATAVFEKPM LPKPVEVEGR VEAFSADLRR NGTEREEESV GPLAWRLKAI EDELQARFDG
MGLPGMTSLP CAGISVNDTS LTSRYSALRR TGPSEPRQGK TLLALNLYNS EDVLPTLSHA
LLTVTSFLDP STVHVSIFEN GSTDKTTLAL AHLAAALTAL GASHTILSDP RKTNWKAVDR
IAQLSVYRNV LLSPLSDSPN SFSDIVFIND VYTCPSDVVE LLFQRKAQEA DAACAMDWRP
NGGIARKWNG SVKFYDNWVS RSLSGETLRA RADILSEWRN GVEEIFDQPG EERWKERWNR
GLPVPVYSCW NGMLALDATP FTSTTISPRY DPSSPLPLSS RKSWRRPPPL TVSTPARFRS
ALKSPGECAA SECKTLAKDF WTRGFDRWLH ETVPLPLPRR TESLKNSLVR PSPLPCAPDH
SACFESIFAL IQPFYIAHTL YRPATTSSYP PEALSRHAKL LARSLGNGSR RRWLPGAWKG
LGLGASLLAV DRTKLDQLSW RELLTCLLSL QLTLRPPARL PSTRASPGFS AEQHRPFQPA
VILPRRPTTT MARSSTDSAP DDSTPETPLL PRYRSDSPPA DGADEKRARR GGAARVKGAW
MDPEDEEDEE DGLGEYRGLR WMQGRRKVGC GVCAVSSARC ILAASILALA AVLAALASLV
YLRHFRTVYR VYEDPLVPDP REVEGMVGRF PRSLARSASE MEEPVGPLAW RLQAIEDELQ
ARFDGMGLPG MTSLPCAGIS VNDTSLTSRY SALRQTGPSE PRQGKTLLAL NLYNSEDVLP
TLSHALLTVT SFLDPSTVHV SIFENGSTDN TTLALAHLAA ALTALGASHT ILSDPRKTNW
KAVDRIAQLA VYRNVVLAPL ERDEDFDDIV FINDVFVCPS DILELIFQRK AQEADAACAT
DWIANKGWAS RLNPDVRFYD SWVSRSLSGE TLRRQEDFLA TLRKGVNVLF DQPGEERYKA
RWDKGLPVPV YSCWNGLLAL DAQPFTSTSI SPRYDLSSSL PSSSRKSWPR DSPIASTEPA
RFRSALNNPG ECAASECKLI AKDFWSRGFD RWLVRHFLPS SFERSFDRET LEQIVPSVRV
TYSEPVYSNP SLLSLSSLHP PSPSPTLDAE ERIDWPSYTP PEEVVCWAWT PGPHVDFEWA
RAVWERPYET FAKVLSRG
//
