ID H3SGB2_9BACL Unreviewed; 445 AA.
AC H3SGB2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Class III aminotransferase {ECO:0000313|EMBL:EHQ61922.1};
GN ORFNames=PDENDC454_12835 {ECO:0000313|EMBL:EHQ61922.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ61922.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ61922.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ61922.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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:EHQ61922.1}.
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DR EMBL; AHKH01000028; EHQ61922.1; -; Genomic_DNA.
DR RefSeq; WP_006677066.1; NZ_AHKH01000028.1.
DR AlphaFoldDB; H3SGB2; -.
DR STRING; 1131935.PDENDC454_12835; -.
DR PATRIC; fig|1131935.3.peg.2650; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 1.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EHQ61922.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000003900};
KW Transferase {ECO:0000313|EMBL:EHQ61922.1}.
SQ SEQUENCE 445 AA; 48087 MW; 7A8283B99AA6AEAB CRC64;
MTSIGNERQG VNQASGIEGN AFIGPEGVLA KRRAYFYPCT QHFYRQPPQI VRGSMQYLYD
HEGRRYTDFF AGVSVVACGH CNPRIAEASV KQLQTLQHTT TIYLTQPMAD LAERLANGIL
PGRLSRTFFC NSGSEANEGA LLLARLHTKR RDFLALEYGL HGRTWLTMGV TGLPMWRADD
HLDEGGVTFI PRPYEPGLDA ETAMRRSLEA LKQALEADPE RYAAMIVEPV QGNGGIIVPP
EGYFREVKAL LEAYGVLLIA DEIQTGFGRT GRMFALDYDG VAPDIVSMAK ALGNGVPIGA
FATTDEIAAS FNRPSASTFG GNPVSSATAL AVLGYIEEEG LVERASRLGE RLKQGLEELQ
RKHQVIADVR GRGLMLGAEL QGAAGTDSAA LTDAVLEAMK ERGFIIGKNG IGRNVLAFQP
PLVIEAGDID AMLEALDDVL GGIEA
//
