ID G8TXW8_SULAD Unreviewed; 376 AA.
AC G8TXW8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN OrderedLocusNames=Sulac_2712 {ECO:0000313|EMBL:AEW06174.1};
OS Sulfobacillus acidophilus (strain ATCC 700253 / DSM 10332 / NAL).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=679936 {ECO:0000313|EMBL:AEW06174.1, ECO:0000313|Proteomes:UP000005439};
RN [1] {ECO:0000313|Proteomes:UP000005439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700253 / DSM 10332 / NAL
RC {ECO:0000313|Proteomes:UP000005439};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R.,
RA Gehrich-Schroeter G., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Sulfobacillus acidophilus DSM
RT 10332.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEW06174.1, ECO:0000313|Proteomes:UP000005439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700253 / DSM 10332 / NAL
RC {ECO:0000313|Proteomes:UP000005439};
RX PubMed=23407703; DOI=10.4056/sigs.2736042;
RA Anderson I., Chertkov O., Chen A., Saunders E., Lapidus A., Nolan M.,
RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Han C., Tapia R.,
RA Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N., Mikhailova N.,
RA Pati A., Palaniappan K., Land M., Pan C., Rohde M., Pukall R., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Mavromatis K.;
RT "Complete genome sequence of the moderately thermophilic mineral-sulfide-
RT oxidizing firmicute Sulfobacillus acidophilus type strain (NAL(T)).";
RL Stand. Genomic Sci. 6:1-13(2012).
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; CP003179; AEW06174.1; -; Genomic_DNA.
DR AlphaFoldDB; G8TXW8; -.
DR STRING; 679936.Sulac_2712; -.
DR KEGG; sap:Sulac_2712; -.
DR PATRIC; fig|679936.5.peg.2806; -.
DR HOGENOM; CLU_028393_2_2_9; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000005439; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005439}.
FT DOMAIN 245..373
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 41
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 139
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 41
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 376 AA; 41071 MW; 965B8C86AE2A7E3A CRC64;
MAIAASLRGT VASVNLGAIQ SNVRRLLQVI GPDVALMAVV KADGYGHGAL PVAQAALAAG
ARWLGVAMAE EGIELREAGV QAPILVLGPN NREQLAAAIR YRLDVVVYSP ESLEWVIEAA
QEVDREARVH LKLDTGMGRI GIPAAGLDEA WLERLSHPRI VWQGLMSHLA DADQDDPASS
REQLKRFLDA VEWLRQKRGS LPPWLHLANS AATLRWPGMH FNLVRVGIAL YGIDPLPGEW
GLRPALSWYS RIAMIKAVEP GTSQGYGRTY RARTAERWAT IPVGYADGYL RGLSNQAAVL
IGGYRCPVIG RVSMDQLVVR LPEALDAHVG DRVTLLGDDG EERLTANHLA EWAGTIGYEI
VTRIGTRVPR EYLEDR
//
