(data stored in ACNUC7421 zone)

SWISSPROT: Q3ILQ1_PSEHT

ID   Q3ILQ1_PSEHT            Unreviewed;       197 AA.
AC   Q3ILQ1;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 83.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS00774032};
DE            EC=2.7.1.25 {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS00774032};
DE   AltName: Full=APS kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00065};
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
GN   Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065,
GN   ECO:0000313|EMBL:CAI85312.1};
GN   OrderedLocusNames=PSHAa0209 {ECO:0000313|EMBL:CAI85312.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85312.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85312.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347,
CC       ECO:0000256|SAAS:SAAS00774005}.
CC   -!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'-
CC       phosphoadenylyl sulfate. {ECO:0000256|HAMAP-Rule:MF_00065,
CC       ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS00774039}.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065,
CC       ECO:0000256|RuleBase:RU004347}.
CC   -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00065, ECO:0000256|RuleBase:RU004347,
CC       ECO:0000256|SAAS:SAAS00774031}.
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DR   EMBL; CR954246; CAI85312.1; -; Genomic_DNA.
DR   RefSeq; WP_011326927.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILQ1; -.
DR   STRING; 326442.PSHAa0209; -.
DR   EnsemblBacteria; CAI85312; CAI85312; PSHAa0209.
DR   KEGG; pha:PSHAa0209; -.
DR   PATRIC; fig|326442.8.peg.200; -.
DR   eggNOG; ENOG4108I67; Bacteria.
DR   eggNOG; COG0529; LUCA.
DR   HOGENOM; HOG000228204; -.
DR   KO; K00860; -.
DR   OMA; VSPFRAD; -.
DR   OrthoDB; POG091H04O4; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-HAMAP.
DR   CDD; cd02027; APSK; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILQ1.
DR   SWISS-2DPAGE; Q3ILQ1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347, ECO:0000256|SAAS:SAAS00774014,
KW   ECO:0000313|EMBL:CAI85312.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|RuleBase:RU004347, ECO:0000313|EMBL:CAI85312.1}.
FT   NP_BIND      32     39       ATP. {ECO:0000256|HAMAP-Rule:MF_00065}.
FT   ACT_SITE    106    106       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00065}.
SQ   SEQUENCE   197 AA;  22138 MW;  1A91571DB70C575E CRC64;
     MDENIVWHNY ATTKAQRSEQ KKHQSAIIWF TGFSGSGKST VANALEAALN QQGIHTYLLD
     GDNVRHGLCK DLGFSDADRV ENIRRVGETA KLMVDAGLLV LTAFISPFRA ERDMVRSLVD
     DKEFIEVFID TPLDVCESRD PKGLYKKARA GEIKHFTGID SSYEIPINPE IILDTSKNTL
     DQSVVQLITY LKQQHII
//

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