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Database: UniProt
Entry: I4AHB0_BERLS
LinkDB: I4AHB0_BERLS
Original site: I4AHB0_BERLS 
ID   I4AHB0_BERLS            Unreviewed;       193 AA.
AC   I4AHB0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|RuleBase:RU004347};
DE            EC=2.7.1.25 {ECO:0000256|RuleBase:RU004347};
GN   OrderedLocusNames=Fleli_0889 {ECO:0000313|EMBL:AFM03345.1};
OS   Bernardetia litoralis (strain ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB
OS   1366 / Fx l1 / Sio-4) (Flexibacter litoralis).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Bernardetiaceae;
OC   Bernardetia.
OX   NCBI_TaxID=880071 {ECO:0000313|EMBL:AFM03345.1, ECO:0000313|Proteomes:UP000006054};
RN   [1] {ECO:0000313|Proteomes:UP000006054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB 1366 / Sio-4
RC   {ECO:0000313|Proteomes:UP000006054};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Lang E., Kopitz M., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Flexibacter litoralis DSM 6794.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|RuleBase:RU004347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC         + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:456216; EC=2.7.1.25;
CC         Evidence={ECO:0000256|RuleBase:RU004347};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 2/3. {ECO:0000256|RuleBase:RU004347}.
CC   -!- SIMILARITY: Belongs to the APS kinase family.
CC       {ECO:0000256|RuleBase:RU004347}.
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DR   EMBL; CP003345; AFM03345.1; -; Genomic_DNA.
DR   RefSeq; WP_014796803.1; NC_018018.1.
DR   AlphaFoldDB; I4AHB0; -.
DR   STRING; 880071.Fleli_0889; -.
DR   KEGG; fli:Fleli_0889; -.
DR   PATRIC; fig|880071.3.peg.868; -.
DR   eggNOG; COG0529; Bacteria.
DR   HOGENOM; CLU_046932_2_2_10; -.
DR   OrthoDB; 9804504at2; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000006054; Chromosome.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR   CDD; cd02027; APSK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00455; apsK; 1.
DR   PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU004347};
KW   Kinase {ECO:0000256|RuleBase:RU004347, ECO:0000313|EMBL:AFM03345.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004347};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006054};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ   SEQUENCE   193 AA;  21815 MW;  A163918D09341E93 CRC64;
     MFPCVIWFIG LSGSGKTTLS DALFEKLKQK YSSTLIKKLD GDLLRNGLNN NLGFSLEDRT
     ENIRRSVEVA KLFYETGFVV LASFITPTHQ NQQLLTDIFD KKRGALFKIF IDCPLEICEQ
     RDVKGLYKKA RTGAIKEFTG ISSPFEKPSS SEVDLIIDSS KLTINESIVL ILDKLEEKGF
     LQKKYFTSAI NNE
//
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