SIRB_ARATH
ID SIRB_ARATH Reviewed; 225 AA.
AC Q84JH7; Q8L8S7; Q9SX37;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Sirohydrochlorin ferrochelatase, chloroplastic {ECO:0000303|PubMed:15545265};
DE Short=AtSirB {ECO:0000303|PubMed:22414210};
DE EC=4.99.1.4 {ECO:0000305|PubMed:15545265};
DE Flags: Precursor;
GN Name=SIRB {ECO:0000303|PubMed:15545265};
GN OrderedLocusNames=At1g50170 {ECO:0000312|Araport:AT1G50170};
GN ORFNames=F14I3.20 {ECO:0000312|EMBL:AAD50047.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=15545265; DOI=10.1074/jbc.m411360200;
RA Raux-Deery E., Leech H.K., Nakrieko K.A., McLean K.J., Munro A.W.,
RA Heathcote P., Rigby S.E., Smith A.G., Warren M.J.;
RT "Identification and characterization of the terminal enzyme of siroheme
RT biosynthesis from Arabidopsis thaliana: a plastid-located sirohydrochlorin
RT ferrochelatase containing a 2FE-2S center.";
RL J. Biol. Chem. 280:4713-4721(2005).
RN [6]
RP FUNCTION, SUBUNIT, CHARACTERIZATION OF IRON-SULFUR CLUSTER, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF CYS-135; CYS-199; CYS-210; CYS-213 AND
RP CYS-219.
RX PubMed=22414210; DOI=10.1042/bj20111993;
RA Saha K., Webb M.E., Rigby S.E., Leech H.K., Warren M.J., Smith A.G.;
RT "Characterization of the evolutionarily conserved iron-sulfur cluster of
RT sirohydrochlorin ferrochelatase from Arabidopsis thaliana.";
RL Biochem. J. 444:227-237(2012).
CC -!- FUNCTION: Chelates iron to the siroheme precursor. Catalyzes the last
CC step of the siroheme biosynthesis. Unlike its counterparts in bacteria,
CC contains an [Fe-S] cluster which is not involved directly in the
CC enzymatic reaction, but may play regulatory role in iron, sulfur and
CC tetrapyrrole metabolism (PubMed:15545265, PubMed:22414210). The [Fe-S]
CC cluster is required for normal plant growth (PubMed:22414210).
CC {ECO:0000269|PubMed:15545265, ECO:0000269|PubMed:22414210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin;
CC Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4;
CC Evidence={ECO:0000305|PubMed:15545265};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24362;
CC Evidence={ECO:0000305|PubMed:15545265};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:15545265, ECO:0000269|PubMed:22414210};
CC Note=Binds 2 [4Fe-4S] clusters per dimer. The [4Fe-4S] cluster quickly
CC oxidizes to a [2Fe-2S] form in the presence of oxygen.
CC {ECO:0000269|PubMed:22414210};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; siroheme from sirohydrochlorin: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22414210}.
CC -!- INTERACTION:
CC Q84JH7; Q9M000: SCL22; NbExp=4; IntAct=EBI-4424960, EBI-4424954;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15545265}.
CC -!- DISRUPTION PHENOTYPE: Post-germination growth arrest.
CC {ECO:0000269|PubMed:22414210}.
CC -!- SIMILARITY: Belongs to the CbiX family. SirB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50047.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007980; AAD50047.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32521.1; -; Genomic_DNA.
DR EMBL; BT004060; AAO42090.1; -; mRNA.
DR EMBL; BT005145; AAO50678.1; -; mRNA.
DR EMBL; AY088838; AAM67145.1; -; mRNA.
DR PIR; A96538; A96538.
DR RefSeq; NP_564562.1; NM_103902.4.
DR AlphaFoldDB; Q84JH7; -.
DR SMR; Q84JH7; -.
DR IntAct; Q84JH7; 1.
DR STRING; 3702.AT1G50170.1; -.
DR PaxDb; Q84JH7; -.
DR PRIDE; Q84JH7; -.
DR ProteomicsDB; 232535; -.
DR EnsemblPlants; AT1G50170.1; AT1G50170.1; AT1G50170.
DR GeneID; 841439; -.
DR Gramene; AT1G50170.1; AT1G50170.1; AT1G50170.
DR KEGG; ath:AT1G50170; -.
DR Araport; AT1G50170; -.
DR TAIR; locus:2011987; AT1G50170.
DR eggNOG; ENOG502RXIW; Eukaryota.
DR HOGENOM; CLU_065901_1_0_1; -.
DR InParanoid; Q84JH7; -.
DR OrthoDB; 1512237at2759; -.
DR PhylomeDB; Q84JH7; -.
DR BRENDA; 4.99.1.4; 399.
DR UniPathway; UPA00262; UER00376.
DR PRO; PR:Q84JH7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84JH7; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IDA:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0019354; P:siroheme biosynthetic process; IDA:TAIR.
DR InterPro; IPR002762; CbiX-like.
DR Pfam; PF01903; CbiX; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Lyase; Metal-binding; Plastid;
KW Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..225
FT /note="Sirohydrochlorin ferrochelatase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435491"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O29537"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O29537"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:22414210"
FT BINDING 210
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:22414210"
FT BINDING 213
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:22414210"
FT BINDING 219
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:22414210"
FT MUTAGEN 135
FT /note="C->A: No effect on the [4Fe-4S] cluster binding. No
FT effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22414210"
FT MUTAGEN 199
FT /note="C->A: Impairs [4Fe-4S] cluster binding. No effect on
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22414210"
FT MUTAGEN 210
FT /note="C->A: Impairs [4Fe-4S] cluster binding. No effect on
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22414210"
FT MUTAGEN 213
FT /note="C->A: Impairs [4Fe-4S] cluster binding. No effect on
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22414210"
FT MUTAGEN 219
FT /note="C->A: Impairs [4Fe-4S] cluster binding. No effect on
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22414210"
FT CONFLICT 109
FT /note="E -> D (in Ref. 4; AAM67145)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="P -> R (in Ref. 4; AAM67145)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="N -> K (in Ref. 4; AAM67145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 24925 MW; B0B64F1303184827 CRC64;
MTTQSQFLVN LSYGGLASQS NLRANNRVSP SSCQITRTNR SWALPVSFKV EKFQLQRGRR
RRGSPCFGES EGLVKNGIGD ADGIIIVDHG SRRRESNLML EEFVKMFKEK TGYPIVEPAH
MELAEPSIKD AFSLCVQQGA KRVVVSPFFL FPGRHWHTDI PSLTADAAKE FSGISYLITA
PLGPHNLLLD VVNDRIQHCL SHVEGDADEC LVCAGTNKCK LYNSS
