ID A0A1I2CUY9_9FLAO Unreviewed; 451 AA.
AC A0A1I2CUY9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=UDP-N-acetylmuramate: L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000313|EMBL:SFE72121.1};
GN ORFNames=SAMN04488131_103188 {ECO:0000313|EMBL:SFE72121.1};
OS Flavobacterium xueshanense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=935223 {ECO:0000313|EMBL:SFE72121.1, ECO:0000313|Proteomes:UP000198596};
RN [1] {ECO:0000313|EMBL:SFE72121.1, ECO:0000313|Proteomes:UP000198596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9227 {ECO:0000313|EMBL:SFE72121.1,
RC ECO:0000313|Proteomes:UP000198596};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FONQ01000003; SFE72121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2CUY9; -.
DR STRING; 935223.SAMN04488131_103188; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000198596; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000713; Mur_ligase_N.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:SFE72121.1}.
FT DOMAIN 2..102
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 108..280
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 451 AA; 50699 MW; 9F3036D36F73C436 CRC64;
MHTHFIAIGG SAMHNLALAL HNKGYQVTGS DDAIFEPSKS RLDKKGILPP VLGWFPEKIT
KDIEAVILGM HAKEDNPELL KAQELGLKIY SYPEFLYEQS KNKTRVVIGG SHGKTTITSM
ILHVMHYHNI AVDYMVGAQL EGFDTMVHLT EENDFIVLEG DEYLSSPIDR RPKFHLYQPN
IALISGIAWD HINVFPTYEN YVEQFEIFIG KITNGGILVY NEDDTEVKRV SEAATNPIRK
LAYHTPKYSV SDGVTLLETP EGDMPIEVFG AHNLNNLAGA KWICQNMGVD EADFYEAIAS
FKGASKRLEK IAESKTKVAY KDFAHSPSKV AATTKAVKEQ YPNRTLVACL ELHTYSSLNA
EFLKEYEGAL EYADKAVVFY SPDAVKIKQL EEVTYDQIAN AFNRKDLIIY TNPKDFKDYL
FNLNLENTAL LLMSSGNYGG LNFDEVKEVI K
//
