ID D8GII9_CLOLD Unreviewed; 385 AA.
AC D8GII9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN Name=alr3 {ECO:0000313|EMBL:ADK17063.1};
GN OrderedLocusNames=CLJU_c40390 {ECO:0000313|EMBL:ADK17063.1};
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK17063.1, ECO:0000313|Proteomes:UP000001656};
RN [1] {ECO:0000313|EMBL:ADK17063.1, ECO:0000313|Proteomes:UP000001656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC
RC {ECO:0000313|Proteomes:UP000001656};
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform based
RT on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; CP001666; ADK17063.1; -; Genomic_DNA.
DR RefSeq; WP_013240628.1; NZ_LITS01000020.1.
DR AlphaFoldDB; D8GII9; -.
DR STRING; 748727.CLJU_c40390; -.
DR KEGG; clj:CLJU_c40390; -.
DR PATRIC; fig|748727.19.peg.1296; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_9; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000001656; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_01201; Ala_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; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00492; alr; 1.
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.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}.
FT DOMAIN 245..373
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 38
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 266
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 38
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 385 AA; 42693 MW; A68A771836F912F5 CRC64;
MLTNHRPVWV EVDLSIIASN MRSIRDVCKD KEIFGVVKAD AYGHGAIDVA PVLLENGATR
LAVALVSEGI ELRKAGVTCQ INVLGITPPN LFRELLEYEL EPVVSDYDYA KALSESAAAL
NKTVRIHLKV DTGLGRIGFL TTEKAVDEAV MISKLPNIFI ESIFSHFSSA GEANKEYSYK
QFEKFQWFIN KMEEKGLYIK LKHIANSSAI WNLPETYLDG VRPGTIIYGC SSDDVKREVI
PIKPAMTWKA NILFLKELEA GQYIGYGRKF RTERKSIIGT LGVGYADGYS RMLSGKAKVI
INGKFAPVVG NICMDQCMVD LTDIGDVKLG DEVILMGSQG ELKIDADDIA KLIGTNNNEV
MCLIGRRVPR VYIKDGKVIK IKNNF
//
