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Database: UniProt
Entry: U6GN22_EIMAC
LinkDB: U6GN22_EIMAC
Original site: U6GN22_EIMAC 
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}.
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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
//
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