ID   A7I0H7_CAMHC            Unreviewed;       336 AA.
AC   A7I0H7;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Alanine racemase {ECO:0000313|EMBL:ABS51956.1};
DE            EC=5.1.1.1 {ECO:0000313|EMBL:ABS51956.1};
GN   OrderedLocusNames=CHAB381_0420 {ECO:0000313|EMBL:ABS51956.1};
OS   Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS   CH001A).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360107 {ECO:0000313|EMBL:ABS51956.1, ECO:0000313|Proteomes:UP000002407};
RN   [1] {ECO:0000313|Proteomes:UP000002407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A
RC   {ECO:0000313|Proteomes:UP000002407};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT   commensal isolated from the human gastrointestinal tract.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600821-50};
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DR   EMBL; CP000776; ABS51956.1; -; Genomic_DNA.
DR   RefSeq; WP_012108301.1; NC_009714.1.
DR   AlphaFoldDB; A7I0H7; -.
DR   STRING; 360107.CHAB381_0420; -.
DR   KEGG; cha:CHAB381_0420; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_7; -.
DR   OrthoDB; 9813814at2; -.
DR   Proteomes; UP000002407; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABS51956.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR600821-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002407}.
FT   DOMAIN          224..336
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         33
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   336 AA;  37795 MW;  F06EF1E8E8158DC6 CRC64;
     MSEILLDKSA FLSNLTKISQ KLGGKEKIML IAKDNSYGHG SAQIAGIARE FGIKKAVVKS
     EMEAEQIAEF YDEILILSHI PTGCEKPDFS YAINDMSHFS KIKNGSKVHI SVDTLMHRNG
     ILPEQLDDAL RLVRENHLNL GGFYTHFRAS DEIGSDFFVQ RENWRNFKIS AQKKCKNLGF
     NVVFHSCNSA AIERSEEFSD DFARVGMAQF GYFQFSEILG LKPVLSLYAD RISSRLLKKG
     ERVGYGGVFE APCDILISTY DLGYGDGLLR YNGKGDLRLG NNEKILGKMS MDSFASKDAG
     ERVCVFDDAR VWARFFNTIE YEILVKLSAN IKRTVK
//