(data stored in SCRATCH917 zone)

HOGENOM: FERNB_1_PE1001

ID   FERNB_1_PE1001                       STANDARD;      PRT;   364 AA.
AC   FERNB_1_PE1001; A7HLU1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Alanine racemase; EC=5.1.1 1; (FERNB_1.PE1001).
GN   Name=alr; OrderedLocusNames=Fnod_1025;
OS   FERVIDOBACTERIUM NODOSUM RT17-B1.
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Fervidobacterium.
OX   NCBI_TaxID=381764;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FERNB_1.PE1001.
CC       Fervidobacterium nodosum Rt17-B1 chromosome, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:A7HLU1_FERNB
CC   -!- FUNCTION: Provides the D-alanine required for cell wall
CC       biosynthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC   -!- GENE_FAMILY: HOG000031444 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A7HLU1; -.
DR   EMBL; CP000771; ABS60874.1; -; Genomic_DNA.
DR   RefSeq; YP_001410531.1; NC_009718.1.
DR   ProteinModelPortal; A7HLU1; -.
DR   STRING; A7HLU1; -.
DR   GeneID; 5452640; -.
DR   GenomeReviews; CP000771_GR; Fnod_1025.
DR   KEGG; fno:Fnod_1025; -.
DR   eggNOG; COG0787; -.
DR   OMA; VPRVYLN; -.
DR   ProtClustDB; CLSK975944; -.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:HAMAP.
DR   GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   Gene3D; G3DSA:2.40.37.10; Ala_racemase/Decarboxylase_C; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SUPFAM; SSF50621; Racem_decarbox_C; 1.
DR   TIGRFAMs; TIGR00492; Alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
DR   HOGENOMDNA; FERNB_1.PE1001; -.
KW   alanine racemase;
KW   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Isomerase; Peptidoglycan synthesis; Pyridoxal phosphate.
SQ   SEQUENCE   364 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MESRRTYAVI NVRNYLDNLR FFQTHCAPAK VMPVVKANAY GHGAVQLAKA AQKIGIDYFA
     VAFLEEAIEL RKHGISKDIL VFNYIEPDLL HIAMENNITI TLYSWEQLWK YTKYVWRPKA
     HIKIDTGMRR LGVYPEEAKD FIESARNVGF EVEGAYTHFA VADSLDDEDV KFTQQQVEKF
     ANLNLDVKIK HLCNSGASVS KIVNCFDYVR VGIASYGLQP SDSVYSEQLK PVLSWKTTVS
     HVKTIQPGDS VSYGRTFKAF TEMRIATIPV GYADGYWRHL SNKGYVLIHG EKCPIIGRVC
     MDQFMVDVTH LEDVKIGDEV ILIGKQGDNI ITAEEIAKLV GTINYEVTCR ISERVPRKYE
     GLEL
//

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