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Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase)

 A0A0A8WQR1_9DELT        Unreviewed;       454 AA.
A0A0A8WQR1;
04-MAR-2015, integrated into UniProtKB/TrEMBL.
04-MAR-2015, sequence version 1.
27-SEP-2017, entry version 18.
RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834};
AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
Short=DAPA AT {ECO:0000256|HAMAP-Rule:MF_00834};
Short=DAPA aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834};
Short=DANS {ECO:0000256|HAMAP-Rule:MF_00834};
AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834};
Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834,
ECO:0000313|EMBL:GAM09970.1};
ORFNames=OR1_02255 {ECO:0000313|EMBL:GAM09970.1};
Geobacter sp. OR-1.
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
Geobacteraceae; Geobacter.
NCBI_TaxID=1266765 {ECO:0000313|EMBL:GAM09970.1, ECO:0000313|Proteomes:UP000030972};
[1] {ECO:0000313|EMBL:GAM09970.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM09970.1,
ECO:0000313|Proteomes:UP000030972};
PubMed=23668621; DOI=10.1021/es400231x;
Ohtsuka T., Yamaguchi N., Makino T., Sakurai K., Kimura K., Kudo K.,
Homma E., Dong DT., Amachi S.;
"Arsenic dissolution from Japanese paddy soil by a dissimilatory
arsenate-reducing bacterium Geobacter sp. OR-1.";
Environ. Sci. Technol. 47:6263-6271(2013).
[2] {ECO:0000313|EMBL:GAM09970.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM09970.1,
ECO:0000313|Proteomes:UP000030972};
Ehara A., Suzuki H., Amachi S.;
"Draft Genome Sequence of Geobacter sp. Strain OR-1, an Arsenate-
Respiring Bacterium Isolated from Japanese Paddy Soil.";
Genome Announc. 3:e01478-14(2015).
-!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S-
adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid
(KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
animotransferase known to utilize SAM as an amino donor.
{ECO:0000256|HAMAP-Rule:MF_00834}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
diaminononanoate. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000256|HAMAP-Rule:MF_00834};
-!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
1/1. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP-
Rule:MF_00834}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00834}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:GAM09970.1}.
-----------------------------------------------------------------------
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EMBL; BAZF01000009; GAM09970.1; -; Genomic_DNA.
RefSeq; WP_041971914.1; NZ_BAZF01000009.1.
EnsemblBacteria; GAM09970; GAM09970; OR1_02255.
UniPathway; UPA00078; UER00160.
Proteomes; UP000030972; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-UniRule.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
HAMAP; MF_00834; BioA; 1.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR005815; BioA.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00202; Aminotran_3; 1.
PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR00508; bioA; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
3: Inferred from homology;
Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834,
ECO:0000313|EMBL:GAM09970.1};
Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
Complete proteome {ECO:0000313|Proteomes:UP000030972};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834,
ECO:0000256|RuleBase:RU003560};
Reference proteome {ECO:0000313|Proteomes:UP000030972};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834};
Transferase {ECO:0000256|HAMAP-Rule:MF_00834,
ECO:0000313|EMBL:GAM09970.1}.
REGION 119 120 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00834}.
BINDING 152 152 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 260 260 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 289 289 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
BINDING 324 324 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00834}.
BINDING 419 419 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00834}.
SITE 22 22 Participates in the substrate recognition
with KAPA and in a stacking interaction
with the adenine ring of SAM.
{ECO:0000256|HAMAP-Rule:MF_00834}.
MOD_RES 289 289 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_00834}.
SEQUENCE 454 AA; 50777 MW; AA6D28BF1329064E CRC64;
MSDINDTRTL REYDRKHIWH PFTQMREWEE SDPIVIVRGE GCWLIDSLGN RYLDGVGSIW
TNVHGHAVPE INQAVKDQLD RIEHATLLGL ANDKAAILAK RLVDIAPPGL TKVFYSDNGS
TAVEIGLKMA FQYWQHKGRP EKTRFISFRN AYHGDTIGAV SVGGIDIFHA VFNPLLFKAV
HAPSPYCYHC ELCLEKNHAD CNRECLNELE RLITANANEL AGLVIEPLVQ GAGGMIVQPP
GFLKRIRELC DRFELLMIAD EVAVGFGRTG SMFACQQEGV TPDIMALSKG ITGGYLPLAA
TMTTKEIYNA FLGEYREMKT FFHGHTFTGN PVCCAAALAS LDLFEENRLI EALEPKIEYL
SERLNSLSKL QHVGNVRQCG MIAGIEMVRD KTTREPYNWE ERVGMQICQE AKNHGLFLRP
LGNVIVVFPP LVISLEELKF LLDGIETSII NICG


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