(data stored in SCRATCH zone)

SWISSPROT: D7A017_STAND

ID   D7A017_STAND            Unreviewed;       408 AA.
AC   D7A017;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=5-aminolevulinate synthase {ECO:0000256|RuleBase:RU910713};
DE            EC=2.3.1.37 {ECO:0000256|RuleBase:RU910713};
DE   AltName: Full=5-aminolevulinic acid synthase {ECO:0000256|RuleBase:RU910713};
DE   AltName: Full=Delta-ALA synthase {ECO:0000256|RuleBase:RU910713};
DE   AltName: Full=Delta-aminolevulinate synthase {ECO:0000256|RuleBase:RU910713};
GN   OrderedLocusNames=Snov_0094 {ECO:0000313|EMBL:ADH87431.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87431.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87431.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 +
CC         CoA; Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:356416; EC=2.3.1.37;
CC         Evidence={ECO:0000256|RuleBase:RU910713};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU003693,
CC         ECO:0000256|SAAS:SAAS00612749};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC       {ECO:0000256|RuleBase:RU910713}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR   EMBL; CP002026; ADH87431.1; -; Genomic_DNA.
DR   RefSeq; WP_013164936.1; NC_014217.1.
DR   STRING; 639283.Snov_0094; -.
DR   EnsemblBacteria; ADH87431; ADH87431; Snov_0094.
DR   KEGG; sno:Snov_0094; -.
DR   eggNOG; ENOG4107EEK; Bacteria.
DR   eggNOG; COG0156; LUCA.
DR   HOGENOM; HOG000221020; -.
DR   KO; K00643; -.
DR   OMA; EHANKQI; -.
DR   OrthoDB; 479874at2; -.
DR   BioCyc; SNOV639283:G1GLM-94-MONOMER; -.
DR   UniPathway; UPA00251; UER00375.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0003870; F:5-aminolevulinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01821; 5aminolev_synth; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D7A017.
DR   SWISS-2DPAGE; D7A017.
KW   Acyltransferase {ECO:0000256|RuleBase:RU910713,
KW   ECO:0000313|EMBL:ADH87431.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Heme biosynthesis {ECO:0000256|RuleBase:RU910713};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003693,
KW   ECO:0000256|SAAS:SAAS00473492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
KW   Transferase {ECO:0000256|RuleBase:RU910713,
KW   ECO:0000313|EMBL:ADH87431.1}.
FT   DOMAIN       46    389       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
SQ   SEQUENCE   408 AA;  43895 MW;  20F5E2C256F1A7CA CRC64;
     MDYARFFQNA VDTLKQERRY RTFAEIERDS ARFPHAVWHS PQGARDIVIW CSNDYLGMGC
     HETVVEAMCA TARQAGAGAG GTRNISGNSH AIVELEAELA DLHGKDAALV FTSGYVSNQT
     GISTLAKLIP DCLVLSDALN HNSMIEGVRQ AGRDKQIFRH NDLAHLEELL KAAGDRPKLV
     VFESVYSMDG DVAPIGAICD LAERYNAMTY LDEVHAVGMY GPRGAGVAER DGVMHRVDVI
     EGTLGKAFGV VGGYITASRA IVDAVRSYAP GFIFTTALPP AVAAAAAASV RHLKASGTER
     TRQQAQVAKV KRALDLAGLP QIVTDTHIVP VMVGDAEACK AASDMLLADH GIYIQPINYP
     TVPRGSERLR ITPGPFHDDA LVAQLAHALV DVWSRLGLPF VTRAEAAE
//

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