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Database: UniProt
Entry: A0A2U3VEP8_ODORO
LinkDB: A0A2U3VEP8_ODORO
Original site: A0A2U3VEP8_ODORO 
ID   A0A2U3VEP8_ODORO        Unreviewed;       714 AA.
AC   A0A2U3VEP8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Propionate--CoA ligase {ECO:0000256|ARBA:ARBA00029726};
DE            EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
DE            EC=6.2.1.17 {ECO:0000256|ARBA:ARBA00012985};
GN   Name=ACSS2 {ECO:0000313|RefSeq:XP_004393143.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004393143.1};
RN   [1] {ECO:0000313|RefSeq:XP_004393143.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC         Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC         ChEBI:CHEBI:456215; EC=6.2.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000787};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC         Evidence={ECO:0000256|ARBA:ARBA00000787};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001884};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC         Evidence={ECO:0000256|ARBA:ARBA00001884};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   RefSeq; XP_004393143.1; XM_004393086.1.
DR   AlphaFoldDB; A0A2U3VEP8; -.
DR   STRING; 9708.A0A2U3VEP8; -.
DR   GeneID; 101373113; -.
DR   KEGG; oro:101373113; -.
DR   CTD; 55902; -.
DR   InParanoid; A0A2U3VEP8; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000245340; Unplaced.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05966; ACS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR032387; ACAS_N.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR24095:SF126; ACETYL-COENZYME A SYNTHETASE, CYTOPLASMIC; 1.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245340}.
FT   DOMAIN          47..107
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          116..541
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          596..674
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   714 AA;  80748 MW;  06D518E2AD97046D CRC64;
     MGLPEERGRS GSRSAEREEA GARNRVRSWS PPPKVSRSAH VRSLQRYREL HRRSVEQPRE
     FWGDIAKEFY WKTSCPGPFL RYNFDVTKGK IFIEWMKGAT TNICYNVLDR IVHEKKLGDK
     VAFYWEGNEP EETTQITYRE LLVQVCRFSN VLQKQGIRKG DRVAIYMPMI PELVVAMLAC
     ARLGALHSIV FAGFSAESLC ERILDSSCSL LITTDAFYRG EKLVNLKELA DEALEKCREK
     AFQVRCCIVV KHLGRAELGT GDSPSQSPPI KRPCPDVQGK LREKPKRIWP QISWNQGVDL
     WWHELMQEAE DECEPEWCDA EDPLFILYTS GSTGKPKGVV HTLGGYMLYV ATTFKYVFDF
     HAEDVFWCTA DIGWITGHSY VTYGPLANGA TSVLFEGIPT YPDVSRLWNI VDKYKVTKFY
     TAPTAIRLLM KFGNEPVTRH SRASLQVLGT VGEPINPEAW LWYHQVVGAQ RCSIVDTFWQ
     TETGGHMLTP LPGATPMKPG SATFPFFGVA PAILNESGEE LEGEAEGYLV FKQPWPGIMR
     TVYGNHERFE ATYFKKFPGY YVTGDGCRRD QDGYYWITGR IDDMLNVSGH LLSTAEVESA
     LVEHEAIAEA AVVGHPHPVK GECLYCFVTL CDGYTFSPTL TEELKKQIRE KIGPIATPDY
     IQNAPGLPKT RSGKIMRRVL RKIAQNDHDL GDMSTVADPT VICQLFNHRC LTSQ
//
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