(data stored in SCRATCH zone)

SWISSPROT: Q2IM15_ANADE

ID   Q2IM15_ANADE            Unreviewed;       457 AA.
AC   Q2IM15;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE            EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834};
DE   AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE            Short=DAPA AT {ECO:0000256|HAMAP-Rule:MF_00834};
DE            Short=DAPA aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE   AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834};
DE            Short=DANS {ECO:0000256|HAMAP-Rule:MF_00834};
DE   AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834};
GN   Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834};
GN   OrderedLocusNames=Adeh_0069 {ECO:0000313|EMBL:ABC79847.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79847.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC79847.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC79847.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
CC       adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid
CC       (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
CC       animotransferase known to utilize SAM as an amino donor.
CC       {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-amino-7-oxononanoate + S-adenosyl-L-methionine = 7,8-
CC         diaminononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate;
CC         Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490, ChEBI:CHEBI:57532,
CC         ChEBI:CHEBI:58500, ChEBI:CHEBI:59789; EC=2.6.1.62;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC       diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00834}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00834}.
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; CP000251; ABC79847.1; -; Genomic_DNA.
DR   RefSeq; WP_011419130.1; NC_007760.1.
DR   STRING; 290397.Adeh_0069; -.
DR   EnsemblBacteria; ABC79847; ABC79847; Adeh_0069.
DR   KEGG; ade:Adeh_0069; -.
DR   eggNOG; ENOG4108JPX; Bacteria.
DR   eggNOG; COG0161; LUCA.
DR   HOGENOM; HOG000020209; -.
DR   KO; K00833; -.
DR   OMA; NGSSCIE; -.
DR   BioCyc; ADEH290397:G1G5W-72-MONOMER; -.
DR   UniPathway; UPA00078; UER00160.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00834; BioA; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR005815; BioA.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00508; bioA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IM15.
DR   SWISS-2DPAGE; Q2IM15.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:ABC79847.1};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:ABC79847.1}.
FT   REGION      122    123       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING     155    155       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     261    261       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     290    290       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     325    325       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING     420    420       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   SITE         25     25       Participates in the substrate recognition
FT                                with KAPA and in a stacking interaction
FT                                with the adenine ring of SAM.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   MOD_RES     290    290       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
SQ   SEQUENCE   457 AA;  50109 MW;  8FD16FC632E94272 CRC64;
     MEDRERQERH RRLWEADHRH LWHPFTQMKD WLREEPLIVD AAEGVYLVDT LGNRYLDGVS
     SLWCNVHGHR VPELDAAVRA QLDRVAHSTL LGLASTASIE CAEELVRHLP PGLTRVFFSD
     AGATAVEIAI KMAFQHHQLR GDERRTEFVA LHGGYHGDTI GSVSVGGIDL FHRIFKPLLF
     EVHHAPQPYC YRCPLGKALP GCGMACADEV ERIVEAREGR VAALVIEPLV QGADGMITQP
     PGYLRRMREV CDRHGALLVC DEVATGWGRT GTTFAVEQEG VRPDILTMAK GLTGGYLPLA
     ATVTTEQVFE SFLGEHAEKR TFFHGHTYAG NPLACAAATA SMTLFRERGV GAAVPGKAAA
     LARALAPAAR LAHVGEVRQR GLMVGIELVR DRATREEYAY ELRAGDRVTR EARKLGAILR
     PLGNVVVLMP PLAMTEAELT RLAGITLAAI EAATARL
//

If you have problems or comments...

PBIL Back to PBIL home page