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Database: UniProt
Entry: H2CBA1_9LEPT
LinkDB: H2CBA1_9LEPT
Original site: H2CBA1_9LEPT 
ID   H2CBA1_9LEPT            Unreviewed;       229 AA.
AC   H2CBA1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Glutamine amidotransferase class-I {ECO:0000313|EMBL:EHQ05241.1};
GN   ORFNames=Lepil_0537 {ECO:0000313|EMBL:EHQ05241.1};
OS   Leptonema illini DSM 21528.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptonema.
OX   NCBI_TaxID=929563 {ECO:0000313|EMBL:EHQ05241.1, ECO:0000313|Proteomes:UP000005737};
RN   [1] {ECO:0000313|EMBL:EHQ05241.1, ECO:0000313|Proteomes:UP000005737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21528 {ECO:0000313|EMBL:EHQ05241.1,
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.
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DR   EMBL; JH597773; EHQ05241.1; -; Genomic_DNA.
DR   RefSeq; WP_002769689.1; NZ_JH597773.1.
DR   AlphaFoldDB; H2CBA1; -.
DR   STRING; 183.GCA_002009735_00233; -.
DR   HOGENOM; CLU_054974_3_3_12; -.
DR   Proteomes; UP000005737; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01741; GATase1_1; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR044992; ChyE-like.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   PANTHER; PTHR42695; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR   PANTHER; PTHR42695:SF5; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW   ECO:0000313|EMBL:EHQ05241.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005737};
KW   Transferase {ECO:0000313|EMBL:EHQ05241.1}.
FT   DOMAIN          42..181
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        88
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   229 AA;  25376 MW;  21210FA31F6E79C6 CRC64;
     MPSLHIIQHV PFEPAGILPD LARRRGWSVS VTEQFSGDML PQVEKIDRLI VMGGPMGTKD
     EAEFPYLTAE KAFIRAAIAR GTPVLGICLG AQLLAETLGA TVRPNGQKEI GFFSVQKTDA
     ARSSRFFADF PDTFTPLHWH GDTFSLPDGA TQIARTDVCE QQAFEFGPHI GLQFHLEMTP
     ELLAGLIENA RYELVAAPFI MSEAELKEKA GLLKDAHALM VRLFERWLE
//
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