ID A0A251X465_9GAMM Unreviewed; 361 AA.
AC A0A251X465;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN ORFNames=TPSD3_13735 {ECO:0000313|EMBL:OUD12180.1};
OS Thioflexithrix psekupsensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thioflexithrix.
OX NCBI_TaxID=1570016 {ECO:0000313|EMBL:OUD12180.1, ECO:0000313|Proteomes:UP000194798};
RN [1] {ECO:0000313|EMBL:OUD12180.1, ECO:0000313|Proteomes:UP000194798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:OUD12180.1};
RA Fomenkov A., Vincze T., Grabovich M., Anton B.P., Dubinina G., Orlova M.,
RA Belousova E., Roberts R.J.;
RT "Thioflexothrix psekupsii D3 genome sequencing and assembly.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUD12180.1}.
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DR EMBL; MSLT01000023; OUD12180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251X465; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000194798; Unassembled WGS sequence.
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; cd06827; PLPDE_III_AR_proteobact; 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}; Reference proteome {ECO:0000313|Proteomes:UP000194798}.
FT DOMAIN 236..360
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 39
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 257
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 361 AA; 39573 MW; D134766C13451F96 CRC64;
MNKNVFRPTI ATIHLDAILH NYQLIQSLAP NSRIVAVVKA NAYGHGAWPV ARHLAAQAEA
FAVACLEEAL QLRQTGISQP IVLLEGFFSA RELPLIAHHH FIPVFHHHAQ IEQLYSSNVS
QPMDAWIKMD SGMHRLGFAP EKYAAACQRV HDHPCIRSLV AMTHLACADN PDHDFTTQQL
AVFTRYNPLK IKSISNSAGI FTGAESHQEW VRPGIALYGG LPLLAPNEKT EKLRPAMCLS
SKIIAIQEVK AGDRIGYGGD FLCQRNTKAG VVAIGYADGY PRHAPTGTPV WVAGRRVPLI
GRVSMDMISV DLTDHPSAIL GDEVELWGQH LSVNEVAACC KTISYDLLTG VTGRVVFHYS
S
//
