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Database: UniProt
Entry: D0BNI4_9LACT
LinkDB: D0BNI4_9LACT
Original site: D0BNI4_9LACT 
ID   D0BNI4_9LACT            Unreviewed;       405 AA.
AC   D0BNI4;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   13-SEP-2023, entry version 66.
DE   RecName: Full=Arginine deiminase {ECO:0000256|HAMAP-Rule:MF_00242};
DE            Short=ADI {ECO:0000256|HAMAP-Rule:MF_00242};
DE            EC=3.5.3.6 {ECO:0000256|HAMAP-Rule:MF_00242};
DE   AltName: Full=Arginine dihydrolase {ECO:0000256|HAMAP-Rule:MF_00242};
DE            Short=AD {ECO:0000256|HAMAP-Rule:MF_00242};
GN   Name=arcA {ECO:0000256|HAMAP-Rule:MF_00242};
GN   ORFNames=HMPREF0446_01519 {ECO:0000313|EMBL:EEW92449.1};
OS   Granulicatella elegans ATCC 700633.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Granulicatella.
OX   NCBI_TaxID=626369 {ECO:0000313|EMBL:EEW92449.1, ECO:0000313|Proteomes:UP000002939};
RN   [1] {ECO:0000313|EMBL:EEW92449.1, ECO:0000313|Proteomes:UP000002939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700633 {ECO:0000313|EMBL:EEW92449.1,
RC   ECO:0000313|Proteomes:UP000002939};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S.,
RA   Surette M.G., Haas B., Nusbaum C., Birren B.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEW92449.1, ECO:0000313|Proteomes:UP000002939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700633 {ECO:0000313|EMBL:EEW92449.1,
RC   ECO:0000313|Proteomes:UP000002939};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA   Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Granulicatella elegans ATCC 700633.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-arginine = L-citrulline + NH4(+);
CC         Xref=Rhea:RHEA:19597, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:32682, ChEBI:CHEBI:57743; EC=3.5.3.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00001190, ECO:0000256|HAMAP-
CC         Rule:MF_00242};
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005213, ECO:0000256|HAMAP-Rule:MF_00242}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family.
CC       {ECO:0000256|ARBA:ARBA00010206, ECO:0000256|HAMAP-Rule:MF_00242}.
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:EEW92449.1}.
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DR   EMBL; ACRF02000001; EEW92449.1; -; Genomic_DNA.
DR   RefSeq; WP_006703795.1; NZ_KI391971.1.
DR   AlphaFoldDB; D0BNI4; -.
DR   STRING; 626369.HMPREF0446_01519; -.
DR   eggNOG; COG2235; Bacteria.
DR   HOGENOM; CLU_052662_0_1_9; -.
DR   OrthoDB; 9807502at2; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000002939; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016990; F:arginine deiminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.3930.10; Arginine deiminase; 1.
DR   HAMAP; MF_00242; Arg_deiminase; 1.
DR   InterPro; IPR003876; Arg_deiminase.
DR   NCBIfam; TIGR01078; arcA; 1.
DR   PANTHER; PTHR47271; ARGININE DEIMINASE; 1.
DR   PANTHER; PTHR47271:SF2; ARGININE DEIMINASE; 1.
DR   Pfam; PF02274; ADI; 1.
DR   PIRSF; PIRSF006356; Arg_deiminase; 1.
DR   PRINTS; PR01466; ARGDEIMINASE.
DR   SUPFAM; SSF55909; Pentein; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism {ECO:0000256|ARBA:ARBA00022503, ECO:0000256|HAMAP-
KW   Rule:MF_00242}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002939}.
FT   ACT_SITE        395
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00242,
FT                   ECO:0000256|PIRSR:PIRSR006356-1"
SQ   SEQUENCE   405 AA;  45451 MW;  B1D6AB151FD941AA CRC64;
     MSNPIHVFSE IGRLKKVCLH RPGKELENLM PDYLERLLFD DIPYLEDAQK EHDAFAETLR
     NAGVEVLYLE QLAAEAIDAG GVREEFVDEW LSEAGVASVA SQKAIKEHLL SLPTFDLVLK
     TMEGFRKTEV QAEATTLAGM YETDYPFVVD PMPNLYFTRD PFATMANGVS LNHMYADTRN
     RETIYGKYIF TYHPVYGNGK VPFFYNRTED TRIEGGDELV LSKEVLAVGI SQRTDARSIE
     KIAQKLFAET DFKQVLAFVI GENRKFMHLD TVFTHIDYDK FTIHPEIQGG LKVFSITKGE
     NGALNIELTE DKLENVLAKA LGVPSVTLIP CGGGDPVEAA REQWNDGSNT LTIAPGEVVV
     YDRNVVTNAI LEQYGIKLHK IRGSELVRGR GGPRCMSMPF EREDL
//
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