(data stored in ACNUC7421 zone)

SWISSPROT: C6WGQ6_ACTMD

ID   C6WGQ6_ACTMD            Unreviewed;       315 AA.
AC   C6WGQ6;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   SubName: Full=Pyridoxal-5'-phosphate-dependent protein beta subunit {ECO:0000313|EMBL:ACU34372.1};
GN   OrderedLocusNames=Amir_0405 {ECO:0000313|EMBL:ACU34372.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34372.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34372.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|SAAS:SAAS00339553};
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000256|SAAS:SAAS00536520}.
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DR   EMBL; CP001630; ACU34372.1; -; Genomic_DNA.
DR   RefSeq; WP_012783035.1; NC_013093.1.
DR   STRING; 446462.Amir_0405; -.
DR   EnsemblBacteria; ACU34372; ACU34372; Amir_0405.
DR   KEGG; ami:Amir_0405; -.
DR   eggNOG; ENOG4105C7B; Bacteria.
DR   eggNOG; COG1171; LUCA.
DR   HOGENOM; HOG000046974; -.
DR   KO; K01754; -.
DR   OMA; VFGRCLE; -.
DR   OrthoDB; POG091H0FN7; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001926; TrpB-like_PLP-dep.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WGQ6.
DR   SWISS-2DPAGE; C6WGQ6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00418189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   DOMAIN       18    300       PALP. {ECO:0000259|Pfam:PF00291}.
SQ   SEQUENCE   315 AA;  33001 MW;  548B76C21D25EC40 CRC64;
     MDLVTLEDIR AAAERISGAV LRTPLLPWGD GLWLKPESLQ PVGAFKIRGA YNALARLTPE
     DRARGVVAYS SGNHSQAVAR AAREFGVPAV IVIPDNAPEV KVEATRALGA EVVRVPMAER
     ESRALELAAE RGAVLVPPFD HPDVIAGQGT IGLEIVADLP EVATVLVPVS GGGLLSGVAV
     AVKALRPDAR VIGVEPELAA DAGESFAAGR RVDWPAEDRA RTIADGLRAQ PSERTFAHIR
     AHVDGFAAVS EARIRAAVRE LAVRARLVVE PSGATTLAAF LELRERGELG DGPVVAVLSG
     GNVDPALLAE VLREA
//

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