ID D9QQZ6_ACEAZ Unreviewed; 375 AA.
AC D9QQZ6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 80.
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=Acear_1427 {ECO:0000313|EMBL:ADL12937.1};
OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Acetohalobium.
OX NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL12937.1, ECO:0000313|Proteomes:UP000001661};
RN [1] {ECO:0000313|EMBL:ADL12937.1, ECO:0000313|Proteomes:UP000001661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC {ECO:0000313|Proteomes:UP000001661};
RX PubMed=21304692;
RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT 7288).";
RL Stand. Genomic Sci. 3:57-65(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; CP002105; ADL12937.1; -; Genomic_DNA.
DR RefSeq; WP_013278382.1; NC_014378.1.
DR AlphaFoldDB; D9QQZ6; -.
DR STRING; 574087.Acear_1427; -.
DR KEGG; aar:Acear_1427; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_9; -.
DR OMA; HMTHFSD; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000001661; 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:UP000001661}.
FT DOMAIN 246..374
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 40
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 267
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 40
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 375 AA; 41256 MW; 5F4598CDB1C788C7 CRC64;
MGNEFNRPVW VEVNLENIRF NLKQIRARVS ADTLVMAVVK ADAYGHGAVP VARAAVEAGA
DRLAVGLPEE GVQLRNAGFE VPIQILGEVL PEQIPLLAKY GLIPTVSKLE TAVELERINA
QLESRQKIHL KVDTGMGRLG VKPDEVVGFA QKLSSFPHLE LEGLLTHFAT ADEADKEYTR
QQWQKFNYAI ECLEAAGIRI PVKHCANSAA IIDLPEMELD LVRAGIMLYG LRPSDEVGDS
LQLKSVLNWK ARIVYLKEVD KGCGISYGAT YTTADKAEIA TIPLGYADGY FRALSNKGDV
LINGRRAPIR GRVCMDQFMV DVTEIPGVSV GDEVILIGKQ DDKEVTAMEL ADLVGTINYE
IISKITKRVP RIYVN
//