ID U6GN22_EIMAC Unreviewed; 1833 AA.
AC U6GN22;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN ORFNames=EAH_00019060 {ECO:0000313|EMBL:CDI80987.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI80987.1};
RN [1] {ECO:0000313|EMBL:CDI80987.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI80987.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI80987.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI80987.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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 -!- 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 EMBL; HG671427; CDI80987.1; -; Genomic_DNA.
DR RefSeq; XP_013249153.1; XM_013393699.1.
DR EnsemblProtists; CDI80987; CDI80987; EAH_00019060.
DR GeneID; 25269976; -.
DR VEuPathDB; ToxoDB:EAH_00019060; -.
DR OMA; LMDSTAC; -.
DR OrthoDB; 1087103at2759; -.
DR UniPathway; UPA00251; UER00318.
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; cd04823; ALAD_PBGS_aspartate_rich; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 3.
DR InterPro; IPR001731; ALAD.
DR InterPro; IPR030656; ALAD_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11458; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR PANTHER; PTHR11458:SF0; DELTA-AMINOLEVULINIC ACID DEHYDRATASE; 1.
DR Pfam; PF00490; ALAD; 2.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR PRINTS; PR00144; DALDHYDRTASE.
DR SMART; SM01004; ALAD; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
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 Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000515}.
FT DOMAIN 599..757
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 774..822
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 14..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1833 AA; 203271 MW; B47EE06EE08E11A7 CRC64;
MALASMRKAF NEWVSNAGNR GGVPDGAARG DFRGRRLSEP KRRALRGGSD MLEGLDAEED
DGEGDDDEGD EELEPDLDDD DDDIDDNEDD AGYADEEYDP IAPRGPIENN NYGEVWLPIQ
ARPRRNRKDH ATRRLVQESL VKPSSLIYPL FVHDEDISEP ILSLPGHRRL SPADVLKEVD
EARRYGVNAF MLFPKVEDDL KSPLGEESSN PDGLMPRIIM AIKDAFPDAL VLADVALDPY
STSGHDGVVD EDTGTVINDM TVYQICKQLL SGFLNEPFCV SGGDVVPQSV NLARAGADMV
CPSEMMDGRV TAIREALDME GCVDTSILSY ACKYASSLYG PFRDAVGSNM KGSGDKKTYQ
MDISNALEAE REAELDVQEG ADMLMVKPGT PYLDVLRRVR QKTNVPLAAY QVSGEYAMIK
AAAEKGWIDE KATVLETLKG FRRAGADAIA TYYAKDVAKW MAEDCKGSRS FTEPGEQYQL
QEELVAALAP WHFGLPFVER KISLSSTPTA PGGTPAFPLP PPGGGGNNFG EGGGQQLSRP
GYRSTSQLLA SYAPGGKEHA AQLSLAEVGD SATSRLPTAL LPRHPYLQRR LLASGLEVFV
LPHAHPEGSL EVHLEVHAGS TAEADSERGM AHLCEHLVFM GNRKRGEVVA LQGEANAFTD
FHHTVYFVSW RGGERNGTEG RNARKGQEQQ PTGRQDWSPR RLKAALEMMR EVFTAPTQFT
SERLLKEKAA ILSESSLVNT IFYRKEQAQL SKVHSDTILP SRFPIGDMEL LRSWSVEEVR
KFFARFYRPE NATLYIVGDV APLAALRYVD DIIGPVRGDK AGEEEWRVIR SRWLQRTVKK
HSVFFPPLTH AWTRESETVD ASANPEWTNT GETPALGVFF EGTHSTAASL GSLLRPRLHV
WQHSLLQHFS LLFLRKLPLA ALRTTGDFFR LLARKLALQA LAIRFTERCR REDDTWMRVE
VADTESVKEG CRIVSVEAEA EQSRWRDAVR VAVEEVRQMA EHGLGEAELA SLLDSYKVNL
DRMHMQLLSS GDMIRLLMDS TACGHRVVHL EDERGLALQL TSGKFGSPNK LASPQAEDAA
AGDRTIAAGS ENLKRLLALV NEEARTMLKW MLTPIEKDRV YSGPDAICAF LVQSGGPQNT
GDNCLPQRRR FPSTQLQGHI AVEQTETGTV KVEGANLPGT PDGERADGDN QTMLAIPEET
ILREVCDAMS RAVPSRKGGV ETPKYLLTNE ELEALRRQAA GFSPVTQRLR EAGPNAQMLQ
FANGAKVTVK PLAEERGSAL IRVLIPGGRL AFMLDSAKGV IDSRGLDNLR EQSAAIMLGA
MTMMEGGAVG PFTRQQIEAF CQERLIGVSI ECMDEFLAID ISAPAFAARD ADSDKAGNYV
RTSTLESAMQ LLHLIFTAFH FEESAFRRAK QRAHMDYHAY TRDLVGYSLG ELIFNMTGGD
PRFDSMKPPV TAGLELPFVE QQMHSHIERQ LARGAIEISV VGDVDSAHVA RLAARYIGTI
THANTNGEGP LKEISSESPA QWSLRSPYYR LQEGSMGAEA PEWSTSRDTE ESLSASHWTK
VWGRRLHAYV RDSEARAVVH IGGFACNRWG RYPNGLWVWD QMEALQRRDD SDAEQMEGKM
FEVKRHGTDE HRKHPAFPRV ALWILQELVT KRLFSILREE QRLTYEAAFD VMSFDILWGG
VFIITVHTQP EEAERVLEAT HLALQQLTSV RPLLQSQLDG AKEQVLSRHL HDRKYARYWL
DLLGGLQLAD VPRKTPAYFS EFERVVKSVT MQDVHLLLRT LGIRRGSVWE AIGVSGPSPP
LALARPPDRI VDAPIASPSS TRLRASEPLR ILS
//