ID A0A0F6AC01_9GAMM Unreviewed; 580 AA.
AC A0A0F6AC01;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Carbamoyltransferase {ECO:0000313|EMBL:KKE82914.1};
GN ORFNames=N479_16010 {ECO:0000313|EMBL:KKE82914.1};
OS Pseudoalteromonas luteoviolacea S4054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE82914.1, ECO:0000313|Proteomes:UP000033434};
RN [1] {ECO:0000313|EMBL:KKE82914.1, ECO:0000313|Proteomes:UP000033434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4054 {ECO:0000313|EMBL:KKE82914.1,
RC ECO:0000313|Proteomes:UP000033434};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
CC -!- SIMILARITY: Belongs to the NodU/CmcH family.
CC {ECO:0000256|ARBA:ARBA00006129}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKE82914.1}.
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DR EMBL; AUXW01000155; KKE82914.1; -; Genomic_DNA.
DR RefSeq; WP_046356720.1; NZ_AUXW01000155.1.
DR AlphaFoldDB; A0A0F6AC01; -.
DR PATRIC; fig|1129367.4.peg.3174; -.
DR Proteomes; UP000033434; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.90.870.20; Carbamoyltransferase, C-terminal domain; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR031730; Carbam_trans_C.
DR InterPro; IPR038152; Carbam_trans_C_sf.
DR InterPro; IPR003696; Carbtransf_dom.
DR PANTHER; PTHR34847; NODULATION PROTEIN U; 1.
DR PANTHER; PTHR34847:SF1; NODULATION PROTEIN U; 1.
DR Pfam; PF16861; Carbam_trans_C; 1.
DR Pfam; PF02543; Carbam_trans_N; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000313|EMBL:KKE82914.1}.
FT DOMAIN 5..356
FT /note="Carbamoyltransferase"
FT /evidence="ECO:0000259|Pfam:PF02543"
FT DOMAIN 410..579
FT /note="Carbamoyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16861"
SQ SEQUENCE 580 AA; 65383 MW; E67C1F070DE70C23 CRC64;
MKYYIGLATS FHDPAIAIVN AKGELIFAED AERFLGYKRG LYCLPDNPYF IEEVLKTHCA
DCTELVIAKT WSKGREKSTN ILENVVLSIL ETFSFNIDVN TRDIKDQFYF ARASQAAAGR
TLSRFFEAGC RNFIVGNYRT KKPTDVRYHD HHLTHAANAC FNSPYDDATC IVVDGMGEKS
SIAYYTYKHG KIKPAPIKVK RSFKSLGLFY TIICENLGFD PLKGEEWKVM GLAPYGKKDQ
KVYDLLRSSL QVKNGNFAVP KNLNAIMKEI KSMAREPGES VERYKDFAYT GQLVFGEIFM
DLINAAYEYA PSKNLCISGG CSLNSSFMGT ALERSKFDNI FVPSAPADDG NAIGAAFLSY
QQDNPSWQPS KTVQSPYTGS TVKEKSLQKL AQYGHLKATD YGDEVYKKTA EFLAQGKIIG
WAQGRAEFGP RSLGNRSILA NPCLPDMKDT INARVKFREE FRPFAPSILH DHGDEYFENY
QESPYMERTL VFREEVRDKV PAVVHVDNTG RLQSVKKEWN EPYYNLISSF KEITGVPVLL
NTSFNIMGKP IVHSVEDMLA VFLMSGIDVL VINNTIYEKS
//
