Carbonic anhydrase - Porphyridium cruentum (Red alga)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Carbonic anhydrase RuleBase RU003956
EC=4.2.1.1 RuleBase RU003956

Gene names

Name:	gtPCA1 EMBL BAA12980.1
Synonyms:	pca1 EMBL BAA92829.1

Organism

Porphyridium cruentum (Red alga) EMBL BAA12980.1

Taxonomic identifier

35688 [NCBI]

Taxonomic lineage

Eukaryota › Rhodophyta › Bangiophyceae › Porphyridiales › Porphyridiaceae › Porphyridium

Protein attributes

Sequence length	571 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	H₂CO₃ = CO₂ + H₂O. RuleBase RU003956
Sequence similarities	Belongs to the beta-class carbonic anhydrase family. RuleBase RU003956

Ontologies

Keywords
Ligand	Metal-binding PDB 1DDZ Zinc RuleBase RU003956 PDB 1DDZ
Molecular function	Lyase RuleBase RU003956 EMBL BAA12980.1
Technical term	3D-structure PDB 1DDZ
Gene Ontology (GO)
Biological process	carbon utilization Inferred from electronic annotation. Source: InterPro
Molecular function	carbonate dehydratase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

149

1

Zinc 1 PDB 1DDZ

Metal binding

151

1

Zinc 1 PDB 1DDZ

Metal binding

205

1

Zinc 1; via tele nitrogen PDB 1DDZ

Metal binding

208

1

Zinc 1 PDB 1DDZ

Metal binding

403

1

Zinc 2 PDB 1DDZ

Metal binding

405

1

Zinc 2 PDB 1DDZ

Metal binding

459

1

Zinc 2; via tele nitrogen PDB 1DDZ

Metal binding

462

1

Zinc 2 PDB 1DDZ

Sequences

Sequence

Length

Mass (Da)

Tools

Q43060 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 05DC7AFFE84F8C87
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FASTA

571

62,095

        10         20         30         40         50         60 
MVQIYNGGAG FERALSRGKS KDGKPKATAA ATAAPAASSS AAPARAAPAR AAPAAAAPVS 

        70         80         90        100        110        120 
KPTAEKPAVA QDATLVKLAA GMGVMSDLEK KFIELEAKLV AQPAGQAMPG KSNIFANNEA 

       130        140        150        160        170        180 
WRQEMLKQDP EFFNRLANGQ SPEYLWIGCA DSRVPANQLL DLPAGEVFVH RNIANQCIHS 

       190        200        210        220        230        240 
DISFLSVLQY AVQYLKVKHI LVCGHYGCGG AKAALGDSRL GLIDNWLRHI RDVRRMNAKY 

       250        260        270        280        290        300 
LDKCKDGDEE LNRLIELNVL EQVHNVCATS IVQDAWDAGQ ELTVQGVVYG VGDGKLRDLG 

       310        320        330        340        350        360 
VVVNSSDDIS KFYRTKSDSG ALKAGNPNAP LVQVTKGGES ELDSTMEKLT AELVQQTPGK 

       370        380        390        400        410        420 
LKEGANRVFV NNENWRQKML KQDPQFFSNL AHTQTPEILW IGCADSRVPA NQIINLPAGE 

       430        440        450        460        470        480 
VFVHRNIANQ CIHSDMSFLS VLQYAVQYLK VKRVVVCGHY ACGGCAAALG DSRLGLIDNW 

       490        500        510        520        530        540 
LRHIRDVRRH NQAELSRITD PKDSLNRLIE INVLEQMHNV CATSIVQDAW DAGQELEVQG 

       550        560        570 
VVYGVGDGKL RDMGVVAKAN DDIGQIFRTK Q

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References

[1]	"Amino acid sequence homology between N- and C-terminal halves of a carbonic anhydrase in Porphyridium purpureum, as deduced from the cloned cDNA." Mitsuhashi S., Miyachi S. J. Biol. Chem. 271:28703-28709(1996) [PubMed: 8910506] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: IAM-R1 EMBL BAA12980.1.
[2]	"X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration." Mitsuhashi S., Mizushima T., Yamashita E., Yamamoto M., Kumasaka T., Moriyama H., Ueki T., Miyachi S., Tsukihara T. J. Biol. Chem. 275:5521-5526(2000) [PubMed: 10681531] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 76-571 IN COMPLEX WITH ZINC.
[3]	"Primary structure of a carbonic anhydrase in Porphyridium purpureum, deduced from the clone cDNA. Amino acid sequence homology between N- and C- terminal halves of the enzyme." Mitsuhashi S., Miyachi S. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: IAM-R1 EMBL BAA12980.1.
[4]	"genomic region coding for a carbonic anhydrase from Porphyridium purpureum." Mitsuhashi S. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D86050 mRNA. Translation: BAA12980.1.
AB040135 Genomic DNA. Translation: BAA92829.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DDZ	X-ray	2.20	A/B	76-571	[»]

ProteinModelPortal

Q43060.

SMR

Q43060. Positions 84-564.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]

Gene3D

G3DSA:3.40.1050.10. CO_anhd_prok_pln. 2 hits.

PANTHER

PTHR11002. Carbonic_anhydrase. 1 hit.

Pfam

PF00484. Pro_CA. 2 hits.
[Graphical view]

SMART

SM00947. Pro_CA. 2 hits.
[Graphical view]

SUPFAM

SSF53056. Prok_plnt_COanhd. 2 hits.

PROSITE

PS00704. PROK_CO2_ANHYDRASE_1. 2 hits.
PS00705. PROK_CO2_ANHYDRASE_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q43060_PORCR

Accession

Primary (citable) accession number: Q43060

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	July 27, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)