ID R9GN34_9SPHI Unreviewed; 413 AA.
AC R9GN34;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=2-amino-3-ketobutyrate coenzyme A ligase {ECO:0000313|EMBL:EOR93111.1};
DE EC=2.3.1.29 {ECO:0000313|EMBL:EOR93111.1};
GN ORFNames=ADIARSV_3732 {ECO:0000313|EMBL:EOR93111.1};
OS Arcticibacter svalbardensis MN12-7.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Arcticibacter.
OX NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR93111.1, ECO:0000313|Proteomes:UP000014174};
RN [1] {ECO:0000313|EMBL:EOR93111.1, ECO:0000313|Proteomes:UP000014174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN12-7 {ECO:0000313|EMBL:EOR93111.1,
RC ECO:0000313|Proteomes:UP000014174};
RX PubMed=23846277;
RA Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT Sample.";
RL Genome Announc. 1:E00484-13(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003693};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOR93111.1}.
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; AQPN01000128; EOR93111.1; -; Genomic_DNA.
DR RefSeq; WP_016196957.1; NZ_AQPN01000128.1.
DR AlphaFoldDB; R9GN34; -.
DR STRING; 1150600.ADIARSV_3732; -.
DR PATRIC; fig|1150600.3.peg.3699; -.
DR eggNOG; COG0156; Bacteria.
DR OrthoDB; 9807157at2; -.
DR Proteomes; UP000014174; Unassembled WGS sequence.
DR GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EOR93111.1};
KW Ligase {ECO:0000313|EMBL:EOR93111.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000014174};
KW Transferase {ECO:0000313|EMBL:EOR93111.1}.
FT DOMAIN 46..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 413 AA; 45832 MW; 828695D5847D6E84 CRC64;
MDLFEKISHN MGPLGQHQKM AHGYFAFPKL EGEIGPHMLF RGKEHLVWSL NNYLGLANHP
EVREADALGA KEFGLAAPMG ARMMSGNSNN HEALEQDLAK FTGKQDAFLL NYGYQGMLSI
IDTLVDRFDV IVYDAECHAC IIDGLRLHMG KRFVYQHNDI ESCKKQLERA TKLAEQTGGA
ILVITEGVFG MSGAQGKIAE IVALKEQFKF RLLIDDAHGF GTMGKTGAGT HEEQNCIDGV
DVYFATFAKS MAGIGAFVAS NETIINYLRY NMRSQTYAKA LPMPMVVGLR KRLELLQSKP
ELREKLWSIA TALQNGLRER GFNLGITNTM VTPVFLKGEL NEATAITMDL RENYGIFCSI
VLYPVIPKGL IELRIIPTAA HTLEDVQVTL DAFSEVAVKL NSGYYKEQNV VKA
//
