ID H2CGI6_9LEPT Unreviewed; 493 AA.
AC H2CGI6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:EHQ07903.1};
GN ORFNames=Lepil_3241 {ECO:0000313|EMBL:EHQ07903.1};
OS Leptonema illini DSM 21528.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptonema.
OX NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ07903.1, ECO:0000313|Proteomes:UP000005737};
RN [1] {ECO:0000313|EMBL:EHQ07903.1, ECO:0000313|Proteomes:UP000005737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ07903.1,
RC ECO:0000313|Proteomes:UP000005737};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The Improved High-Quality Draft genome of Leptonema illini DSM 21528.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; JH597773; EHQ07903.1; -; Genomic_DNA.
DR RefSeq; WP_002774125.1; NZ_JH597773.1.
DR AlphaFoldDB; H2CGI6; -.
DR STRING; 183.GCA_002009735_01258; -.
DR HOGENOM; CLU_016922_1_5_12; -.
DR Proteomes; UP000005737; 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; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
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:EHQ07903.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000005737};
KW Transferase {ECO:0000313|EMBL:EHQ07903.1}.
SQ SEQUENCE 493 AA; 54104 MW; 9D69EE45A7A68843 CRC64;
MKTLETPKRP KTETSQQEYA ISEWHDTDAI HDKLKALLKQ PPRAIRRDKM EQVLAYFEKK
CRKSKAIADE AQRFIPGGVQ HNLAFNHPFP IAIDEANGSF LKDVDGNRYI DFLQAGGPTL
LGSNYAPVRK KIIELLETCG PVTGLLHEYE HKLAEEINRH MPGIEMFRML GSGTEGVMAA
IRLARGYTGK KKIIKVGGAY HGWSDQMVYG MRIPGTGRRE ATGIPGGSTA HTQECFPNDI
GALRRMMMLN RLRGGTAAVI VEPLGPESGT RPIYKNYNAE LRKLCDEFGA LLIFDEVVTG
FRLGMGGAQG YFGVNPDITV FGKCLTGGYP MAGGIGGRRD VMMLLAGGIS AMGKRVFVGG
TLSANPLSCA AGYYTIKEMA RTNAAVKAGQ AGDRLRKGLE DIVDRLGLPY VVYNQGSIVH
LQTSAVLLMS MRNPIKVLKE AKDRKHLMEE MGAAYMSQGI ITLAGSRIYT SMATTDRIVD
DALDRFETVF KMV
//
